4I5D | pdb_00004i5d

Crystal structure of Ralstonia sp. alcohol dehydrogenase in its apo form

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
F [auth E]	d4i5de1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)
F [auth E]	d4i5de2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)
A [auth H]	d4i5dh1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)
A [auth H]	d4i5dh2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)
B [auth A]	d4i5da1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)
B [auth A]	d4i5da2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)
C [auth B]	d4i5db1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)
C [auth B]	d4i5db2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)
D [auth C]	d4i5dc1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)
D [auth C]	d4i5dc2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)
E [auth D]	d4i5dd1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)
E [auth D]	d4i5dd2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)
G [auth F]	d4i5df1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)
G [auth F]	d4i5df2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)
H [auth G]	d4i5dg1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)
H [auth G]	d4i5dg2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Ralstonia sp. DSMZ 6428 ) [TaxId: 517192 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
F [auth E]	SCOP2B Superfamily	SDR-like	8063174	3000038	SCOP2B (2022-06-29)
A [auth H]	SCOP2B Superfamily	SDR-like	8063174	3000038	SCOP2B (2022-06-29)
B [auth A]	SCOP2B Superfamily	SDR-like	8063174	3000038	SCOP2B (2022-06-29)
C [auth B]	SCOP2B Superfamily	SDR-like	8063174	3000038	SCOP2B (2022-06-29)
D [auth C]	SCOP2B Superfamily	SDR-like	8063174	3000038	SCOP2B (2022-06-29)
E [auth D]	SCOP2B Superfamily	SDR-like	8063174	3000038	SCOP2B (2022-06-29)
G [auth F]	SCOP2B Superfamily	SDR-like	8063174	3000038	SCOP2B (2022-06-29)
H [auth G]	SCOP2B Superfamily	SDR-like	8063174	3000038	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
F [auth E]	adh_short_C2	e4i5dE1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
A [auth H]	adh_short_C2	e4i5dH1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
B [auth A]	adh_short_C2	e4i5dA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
C [auth B]	adh_short_C2	e4i5dB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
D [auth C]	adh_short_C2	e4i5dC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
E [auth D]	adh_short_C2	e4i5dD1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
G [auth F]	adh_short_C2	e4i5dF1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
H [auth G]	adh_short_C2	e4i5dG1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
F [auth E]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A [auth H]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
B [auth A]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
C [auth B]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
D [auth C]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
E [auth D]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
G [auth F]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
H [auth G]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth H], B [auth A], C [auth B], D [auth C], E [auth D], A [auth H], B [auth A], C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G]	PF13561	Enoyl-(Acyl carrier protein) reductase (adh_short_C2)	Enoyl-(Acyl carrier protein) reductase	This domain is found in Enoyl-(Acyl carrier protein) reductases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth H], B [auth A], C [auth B], D [auth C], E [auth D], A [auth H], B [auth A], C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G]	Alclohol dehydrogenase/short-chain dehydrogenase	oxidoreductase activity oxidoreductase activity, acting on NAD(P)H catalytic activity oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor binding nucleoside phosphate binding nucleotide binding heterocyclic compound binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth H], B [auth A], C [auth B], D [auth C], E [auth D], A [auth H], B [auth A], C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G]	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A [auth H], B [auth A], C [auth B], D [auth C], E [auth D], A [auth H], B [auth A], C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G]	IPR002347	Short-chain dehydrogenase/reductase SDR	Family

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.