Structure of PDB 5exd Chain G

Receptor sequence
>5exdG (length=394) Species: 264732 (Moorella thermoacetica ATCC 39073) [Search protein sequence]
GKVRNISGCVAVAHGVRLADVDVICSYPIRPYTGIMSELARMVADGELDA
EFVHGEGEHAQLSVVYGASAAGARVFTGSSGVGVTYAMEVYSPISGERLP
VQMAIADRTLDPPGDFGEEHTDAECCRDQGWIQGWASTPQEALDNTLIYY
RVGEDQRVLLPQYACLDGYFVSHILGPVDIPDEAQVKEFLPPYKNHHVLD
PRKPQIIGPQIEPAMGPPLQYQRYQAVKGVHKVLEEACDEFARIFGRKYD
PYLDEYLTDDAEVIIFGQGAHMETAKAVARRLRNLGEKVGVARLRTFRPF
PTEQIKERLSKFKAIGVLDVSANFGISCSGGVLLSELRAALYDYGDKVKT
VGFVAGLGGEVVTHDEFYRMFQKLKEIAKTGKVEQTSYWIPFEL
3D structure
PDB5exd One-carbon chemistry of oxalate oxidoreductase captured by X-ray crystallography.
ChainG
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R31 E59 R109
Catalytic site (residue number reindexed from 1) R30 E58 R108
Enzyme Commision number 1.2.7.10: oxalate oxidoreductase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 TPP G Y28 P29 I30 E59 Y27 P28 I29 E58
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016491 oxidoreductase activity
GO:0016625 oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor
Biological Process
GO:0006979 response to oxidative stress
GO:0033611 oxalate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5exd, PDBe:5exd, PDBj:5exd
PDBsum5exd
PubMed26712008
UniProtQ2RI41|OORA_MOOTA Oxalate oxidoreductase subunit alpha (Gene Name=Moth_1592)

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