6MGJ

Crystal structure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, apoenzyme

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6mgja1	All beta proteins	7-bladed beta-propeller	Oligoxyloglucan reducing end-specific cellobiohydrolase	automated matches	automated matches	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)
A	d6mgja3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)
B	d6mgjb1	All beta proteins	7-bladed beta-propeller	Oligoxyloglucan reducing end-specific cellobiohydrolase	automated matches	automated matches	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)
B	d6mgjb3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)
C	d6mgjc1	All beta proteins	7-bladed beta-propeller	Oligoxyloglucan reducing end-specific cellobiohydrolase	automated matches	automated matches	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)
C	d6mgjc3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)
D	d6mgjd1	All beta proteins	7-bladed beta-propeller	Oligoxyloglucan reducing end-specific cellobiohydrolase	automated matches	automated matches	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)
D	d6mgjd3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)
E	d6mgje1	All beta proteins	7-bladed beta-propeller	Oligoxyloglucan reducing end-specific cellobiohydrolase	automated matches	automated matches	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)
E	d6mgje3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)
F	d6mgjf1	All beta proteins	7-bladed beta-propeller	Oligoxyloglucan reducing end-specific cellobiohydrolase	automated matches	automated matches	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)
F	d6mgjf3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)
G	d6mgjg1	All beta proteins	7-bladed beta-propeller	Oligoxyloglucan reducing end-specific cellobiohydrolase	automated matches	automated matches	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)
G	d6mgjg3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)
H	d6mgjh1	All beta proteins	7-bladed beta-propeller	Oligoxyloglucan reducing end-specific cellobiohydrolase	automated matches	automated matches	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)
H	d6mgjh3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Paenibacillus odorifer ) [TaxId: 189426 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PSII_BNR	e6mgjA2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR	ECOD (1.6)
A	PSII_BNR_1	e6mgjA1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR_1	ECOD (1.6)
B	PSII_BNR	e6mgjB2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR	ECOD (1.6)
B	PSII_BNR_1	e6mgjB1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR_1	ECOD (1.6)
C	PSII_BNR	e6mgjC1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR	ECOD (1.6)
C	PSII_BNR_1	e6mgjC2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR_1	ECOD (1.6)
D	PSII_BNR	e6mgjD2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR	ECOD (1.6)
D	PSII_BNR_1	e6mgjD1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR_1	ECOD (1.6)
E	PSII_BNR	e6mgjE1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR	ECOD (1.6)
E	PSII_BNR_1	e6mgjE2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR_1	ECOD (1.6)
F	PSII_BNR	e6mgjF1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR	ECOD (1.6)
F	PSII_BNR_1	e6mgjF2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR_1	ECOD (1.6)
G	PSII_BNR	e6mgjG1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR	ECOD (1.6)
G	PSII_BNR_1	e6mgjG2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR_1	ECOD (1.6)
H	PSII_BNR	e6mgjH1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR	ECOD (1.6)
H	PSII_BNR_1	e6mgjH2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: PSII_BNR_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.130.10.10	Mainly Beta	7 Propeller	Methylamine Dehydrogenase	Chain H	CATH (4.3.0)
B	2.130.10.10	Mainly Beta	7 Propeller	Methylamine Dehydrogenase	Chain H	CATH (4.3.0)
C	2.130.10.10	Mainly Beta	7 Propeller	Methylamine Dehydrogenase	Chain H	CATH (4.3.0)
D	2.130.10.10	Mainly Beta	7 Propeller	Methylamine Dehydrogenase	Chain H	CATH (4.3.0)
E	2.130.10.10	Mainly Beta	7 Propeller	Methylamine Dehydrogenase	Chain H	CATH (4.3.0)
F	2.130.10.10	Mainly Beta	7 Propeller	Methylamine Dehydrogenase	Chain H	CATH (4.3.0)
G	2.130.10.10	Mainly Beta	7 Propeller	Methylamine Dehydrogenase	Chain H	CATH (4.3.0)
H	2.130.10.10	Mainly Beta	7 Propeller	Methylamine Dehydrogenase	Chain H	CATH (4.3.0)

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.