3ITB

Crystal structure of Penicillin-Binding Protein 6 (PBP6) from E. coli in complex with a substrate fragment

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
C	d3itbc2	All beta proteins	Penicillin-binding protein associated domain	Penicillin-binding protein associated domain	automated matches	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d3itbc1	Multi-domain proteins (alpha and beta)	beta-lactamase/transpeptidase-like	beta-lactamase/transpeptidase-like	automated matches	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d3itba2	All beta proteins	Penicillin-binding protein associated domain	Penicillin-binding protein associated domain	automated matches	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d3itba1	Multi-domain proteins (alpha and beta)	beta-lactamase/transpeptidase-like	beta-lactamase/transpeptidase-like	automated matches	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d3itbb2	All beta proteins	Penicillin-binding protein associated domain	Penicillin-binding protein associated domain	automated matches	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d3itbb1	Multi-domain proteins (alpha and beta)	beta-lactamase/transpeptidase-like	beta-lactamase/transpeptidase-like	automated matches	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d3itbd2	All beta proteins	Penicillin-binding protein associated domain	Penicillin-binding protein associated domain	automated matches	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d3itbd1	Multi-domain proteins (alpha and beta)	beta-lactamase/transpeptidase-like	beta-lactamase/transpeptidase-like	automated matches	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
C	PBP5_C	e3itbC1	A: beta sandwiches	X: Penicillin-binding protein associated domain (From Topology)	H: Penicillin-binding protein associated domain (From Topology)	T: Penicillin-binding protein associated domain	F: PBP5_C	ECOD (1.6)
C	Peptidase_S11_1st	e3itbC2	A: alpha complex topology	X: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)	H: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: alpha-helical domain in beta-lactamase/transpeptidase-like proteins	F: Peptidase_S11_1st	ECOD (1.6)
C	Peptidase_S11_2nd	e3itbC3	A: a+b three layers	X: Profilin-like	H: a+b domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: a+b domain in beta-lactamase/transpeptidase-like proteins	F: Peptidase_S11_2nd	ECOD (1.6)
A	PBP5_C	e3itbA1	A: beta sandwiches	X: Penicillin-binding protein associated domain (From Topology)	H: Penicillin-binding protein associated domain (From Topology)	T: Penicillin-binding protein associated domain	F: PBP5_C	ECOD (1.6)
A	Peptidase_S11_1st	e3itbA2	A: alpha complex topology	X: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)	H: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: alpha-helical domain in beta-lactamase/transpeptidase-like proteins	F: Peptidase_S11_1st	ECOD (1.6)
A	Peptidase_S11_2nd	e3itbA3	A: a+b three layers	X: Profilin-like	H: a+b domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: a+b domain in beta-lactamase/transpeptidase-like proteins	F: Peptidase_S11_2nd	ECOD (1.6)
B	PBP5_C	e3itbB1	A: beta sandwiches	X: Penicillin-binding protein associated domain (From Topology)	H: Penicillin-binding protein associated domain (From Topology)	T: Penicillin-binding protein associated domain	F: PBP5_C	ECOD (1.6)
B	Peptidase_S11_1st	e3itbB2	A: alpha complex topology	X: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)	H: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: alpha-helical domain in beta-lactamase/transpeptidase-like proteins	F: Peptidase_S11_1st	ECOD (1.6)
B	Peptidase_S11_2nd	e3itbB3	A: a+b three layers	X: Profilin-like	H: a+b domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: a+b domain in beta-lactamase/transpeptidase-like proteins	F: Peptidase_S11_2nd	ECOD (1.6)
D	PBP5_C	e3itbD1	A: beta sandwiches	X: Penicillin-binding protein associated domain (From Topology)	H: Penicillin-binding protein associated domain (From Topology)	T: Penicillin-binding protein associated domain	F: PBP5_C	ECOD (1.6)
D	Peptidase_S11_1st	e3itbD2	A: alpha complex topology	X: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)	H: alpha-helical domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: alpha-helical domain in beta-lactamase/transpeptidase-like proteins	F: Peptidase_S11_1st	ECOD (1.6)
D	Peptidase_S11_2nd	e3itbD3	A: a+b three layers	X: Profilin-like	H: a+b domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: a+b domain in beta-lactamase/transpeptidase-like proteins	F: Peptidase_S11_2nd	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	3.40.710.10	Alpha Beta	3-Layer(aba) Sandwich	Beta-lactamase	DD-peptidase/beta-lactamase superfamily	CATH (4.3.0)
C	2.60.410.10	Mainly Beta	Sandwich	Peptidoglycan synthesis regulatory factor (PBP3), Domain 2	D-Ala-D-Ala carboxypeptidase, C-terminal domain	CATH (4.3.0)
A	3.40.710.10	Alpha Beta	3-Layer(aba) Sandwich	Beta-lactamase	DD-peptidase/beta-lactamase superfamily	CATH (4.3.0)
A	2.60.410.10	Mainly Beta	Sandwich	Peptidoglycan synthesis regulatory factor (PBP3), Domain 2	D-Ala-D-Ala carboxypeptidase, C-terminal domain	CATH (4.3.0)
B	3.40.710.10	Alpha Beta	3-Layer(aba) Sandwich	Beta-lactamase	DD-peptidase/beta-lactamase superfamily	CATH (4.3.0)
B	2.60.410.10	Mainly Beta	Sandwich	Peptidoglycan synthesis regulatory factor (PBP3), Domain 2	D-Ala-D-Ala carboxypeptidase, C-terminal domain	CATH (4.3.0)
D	3.40.710.10	Alpha Beta	3-Layer(aba) Sandwich	Beta-lactamase	DD-peptidase/beta-lactamase superfamily	CATH (4.3.0)
D	2.60.410.10	Mainly Beta	Sandwich	Peptidoglycan synthesis regulatory factor (PBP3), Domain 2	D-Ala-D-Ala carboxypeptidase, C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00768	D-alanyl-D-alanine carboxypeptidase (Peptidase_S11)	D-alanyl-D-alanine carboxypeptidase	-	Domain
A, B, C, D	PF07943	Penicillin-binding protein 5, C-terminal domain (PBP5_C)	Penicillin-binding protein 5, C-terminal domain	Penicillin-binding protein 5 expressed by E. coli (Swiss:P04287) functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (Pfam:PF00768) is ...	Penicillin-binding protein 5 expressed by E. coli (Swiss:P04287) functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (Pfam:PF00768) is the catalytic domain. The C-terminal domain featured in this family is organised into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	D-alanyl-D-alanine carboxypeptidase DacC	amide binding organic acid binding binding ion binding organic cyclic compound binding anion binding penicillin binding carboxylic acid binding heterocyclic compound binding monocarboxylic acid binding small molecule binding sulfur compound binding identical protein binding protein binding amide binding organic acid binding binding ion binding organic cyclic compound binding anion binding penicillin binding carboxylic acid binding heterocyclic compound binding monocarboxylic acid binding small molecule binding sulfur compound binding identical protein binding protein binding protein homodimerization activity protein dimerization activity peptidase activity catalytic activity, acting on a protein hydrolase activity exopeptidase activity catalytic activity carboxypeptidase activity serine-type exopeptidase activity serine hydrolase activity serine-type D-Ala-D-Ala carboxypeptidase activity serine-type carboxypeptidase activity serine-type peptidase activity	developmental process regulation of biological process regulation of developmental process biological regulation regulation of cell shape cell morphogenesis regulation of cell morphogenesis anatomical structure morphogenesis anatomical structure development regulation of biological quality regulation of anatomical structure morphogenesis response to stimulus response to chemical response to xenobiotic stimulus developmental process regulation of biological process regulation of developmental process biological regulation regulation of cell shape cell morphogenesis regulation of cell morphogenesis anatomical structure morphogenesis anatomical structure development regulation of biological quality regulation of anatomical structure morphogenesis response to stimulus response to chemical response to xenobiotic stimulus cellular component organization cell wall organization or biogenesis cell wall organization cellular process cellular component organization or biogenesis external encapsulating structure organization carbohydrate derivative biosynthetic process peptidoglycan-based cell wall biogenesis glycosaminoglycan metabolic process carbohydrate derivative metabolic process macromolecule biosynthetic process cellular component biogenesis peptidoglycan biosynthetic process cell wall biogenesis biosynthetic process cell wall macromolecule biosynthetic process aminoglycan metabolic process peptidoglycan metabolic process aminoglycan biosynthetic process metabolic process glycosaminoglycan biosynthetic process macromolecule metabolic process proteolysis primary metabolic process protein metabolic process	cell periphery cellular anatomical structure plasma membrane membrane outer membrane-bounded periplasmic space cell envelope periplasmic space
E [auth L]	Peptidoglycan substrate (AMV)A(FGA)K(DAL)(DAL)	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR012907	Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal	Domain
A, B, C, D	IPR018044	Peptidase S11, D-alanyl-D-alanine carboxypeptidase A	Family
A, B, C, D	IPR012338	Beta-lactamase/transpeptidase-like	Homologous Superfamily
A, B, C, D	IPR015956	Penicillin-binding protein, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR037167	D-Ala-D-Ala carboxypeptidase, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR001967	Peptidase S11, D-alanyl-D-alanine carboxypeptidase A, N-terminal	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
E [auth L]	DAL	RESID: AA0111 , AA0191 PSI-MOD : meso-lanthionine MOD:00120 , D-alanine (Ala) MOD:00198 , D-alanine (Ser) MOD:00858 , D-alanine MOD:00862
E [auth L]	FGA	RESID: AA0111 , AA0191

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.