Structure of PDB 5c4i Chain C

Receptor sequence

>5c4iC (length=312) Species: 264732 (Moorella thermoacetica ATCC 39073)

MLDRIASIKKAPDEEYYVPGHRTCAGCGPALTYRLVAKAAGPNTIFIGPT
GCMYVANTSYGCGPWRVPWIHAQITNGGAVASGIEAAYKAMIRKKKTDAE
FPNIIVMAGDGGAVDIGLQALSAMLYRGHDVLFICYDNESYANTGIQTSP
TTPYGANTTFTPPGEVVPEGKKLFPKDNPKVIAHGHPELKYVATASIGWP
VDLMNKVRKGLNQEGPAYIHIHAPCPKGWQFPADKTIEMAKLAVQTGMFQ
LYEYENGEYKLSVKVDKRKPVSEYMKLQKRFAHLKPEHIAKMQAFVDARC
AEVGITVPVVAS

3D structure

• PDB: 5c4i The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism.
• Chain: C
• Resolution: 2.274 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N143
• Catalytic site (residue number reindexed from 1): N143
• 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	SF4	C	C24 C27 P29 C52 A142 C225 P226 K227	C24 C27 P29 C52 A142 C225 P226 K227
BS02	TPP	C	T50 G51 C52 I74 G109 D110 G111 Y136 N138 S140 Y141 A142 N143 T144	T50 G51 C52 I74 G109 D110 G111 Y136 N138 S140 Y141 A142 N143 T144
BS03	MG	C	D110 N138 S140	D110 N138 S140

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
• GO:0030976 thiamine pyrophosphate binding
• GO:0046872 metal ion binding
• GO:0051539 4 iron, 4 sulfur cluster binding

Biological Process

• GO:0033611 oxalate catabolic process

External links

• PDB: RCSB:5c4i, PDBe:5c4i, PDBj:5c4i
• PDBsum: 5c4i
• PubMed: 26061898
• UniProt: Q2RI42|OORB_MOOTA Oxalate oxidoreductase subunit beta (Gene Name=Moth_1591)