Structure of PDB 5exd Chain L

Receptor sequence
>5exdL (length=310) Species: 264732 (Moorella thermoacetica ATCC 39073) [Search protein sequence]
MLDRIASIKKAPDEEYYVPGHRTCAGCGPALTYRLVAKAAGPNTIFIGPT
GCMYVANTSYGCGPWRVPWIHAQITNGGAVASGIEAAYKAMIRKKKTDAE
FPNIIVMAGDGGAVDIGLQALSAMLYRGHDVLFICYDNESYANTGIQTSP
TTPYGANTTFTPPGEVVPEGKKLFPKDNPKVIAHGHPELKYVATASIGWP
VDLMNKVRKGLNQEGPAYIHIHAPCPKGWQFPADKTIEMAKLAVQTGMFQ
LYEYENGEYKLSVKVDKRKPVSEYMKLQKRFAHLKPEHIAKMQAFVDARC
AEVGITVPVV
3D structure
PDB5exd One-carbon chemistry of oxalate oxidoreductase captured by X-ray crystallography.
ChainL
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) 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 L C24 C27 P29 C52 C225 P226 K227 C24 C27 P29 C52 C225 P226 K227
BS02 TPP L 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 L 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

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Molecular Function

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Biological Process
External links
PDB RCSB:5exd, PDBe:5exd, PDBj:5exd
PDBsum5exd
PubMed26712008
UniProtQ2RI42|OORB_MOOTA Oxalate oxidoreductase subunit beta (Gene Name=Moth_1591)

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