Structure of PDB 7kbl Chain B

Receptor sequence
>7kblB (length=451) Species: 940 (Hydrogenobacter thermophilus) [Search protein sequence]
MFKKVLVANRGEIACRVIRACKELGIQTVAIYNEIESTARHVKMADEAYM
IGVNPLDTYLNAERIVDLALEVGAEAIHPGYGFLAENEHFARLCEEKGIT
FIGPHWKVIELMGDKARSKEVMKRAGVPTVPGSDGILKDVEEAKRIAKEI
GYPVLLKASAGGGGRGIRICRNEEELVRNYENAYNEAVKAFGRGDLLLEK
YIENPKHIEFQVLGDKYGNVIHLGERDCSIQRRNQKLVEIAPSLLLTPEQ
REYYGSLVVKAAKEIGYYSAGTMEFIADEKGNLYFIEMNTRIQVEHPVTE
MITGVDIVKWQIRIAAGERLRYSQEDIRFNGYSIECRINAEDPKKGFAPS
IGTIERYYVPGGFGIRVEHASSKGYEITPYYDSLIAKLIVWAPLWEVAVD
RMRSALETYEISGVKTTIPLLINIMKDKDFRDGKFTTRYLEEHPHVFDYA
E
3D structure
PDB7kbl Structure, Function, and Thermal Adaptation of the Biotin Carboxylase Domain Dimer from Hydrogenobacter thermophilus 2-Oxoglutarate Carboxylase.
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) E274 E287 N289 E295 R337
Catalytic site (residue number reindexed from 1) E274 E287 N289 E295 R337
Enzyme Commision number 6.4.1.7: 2-oxoglutarate carboxylase.
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 BCT B K236 R291 Q293 V294 E295 K236 R291 Q293 V294 E295
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0034029 2-oxoglutarate carboxylase activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:7kbl, PDBe:7kbl, PDBj:7kbl
PDBsum7kbl
PubMed33464881
UniProtD3DJ42|2OCS_HYDTT 2-oxoglutarate carboxylase small subunit (Gene Name=cfiB)

[Back to BioLiP]