Structure of PDB 7kct Chain B

Receptor sequence
>7kctB (length=453) Species: 940 (Hydrogenobacter thermophilus) [Search protein sequence]
HQMFKKVLVANRGEIACRVIRACKELGIQTVAIYNEIESTARHVKMADEA
YMIGVNPLDTYLNAERIVDLALEVGAEAIHPGYGFLAENEHFARLCEEKG
ITFIGPHWKVIELMGDKARSKEVMKRAGVPTVPGSDGILKDVEEAKRIAK
EIGYPVLLKASAGGGGRGIRICRNEEELVRNYENAYNEAVKAFGRGDLLL
EKYIENPKHIEFQVLGDKYGNVIHLGERDCSIQRRNQKLVEIAPSLLLTP
EQREYYGSLVVKAAKEIGYYSAGTMEFIADEKGNLYFIEMNTRIQVEHPV
TEMITGVDIVKWQIRIAAGERLRYSQEDIRFNGYSIECRINAEDPKKGFA
PSIGTIERYYVPGGFGIRVEHASSKGYEITPYYDSLIAKLIVWAPLWEVA
VDRMRSALETYEISGVKTTIPLLINIMKDKDFRDGKFTTRYLEEHPHVFD
YAE
3D structure
PDB7kct Structure, Function, and Thermal Adaptation of the Biotin Carboxylase Domain Dimer from Hydrogenobacter thermophilus 2-Oxoglutarate Carboxylase.
ChainB
Resolution2.02 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E274 E287 N289 E295 R337
Catalytic site (residue number reindexed from 1) E276 E289 N291 E297 R339
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 ADP B K236 R291 Q293 V294 E295 R337 D382 K238 R293 Q295 V296 E297 R339 D384
BS02 ADP B K115 L155 K157 G162 G163 G164 I167 E199 Y201 I202 H207 Q231 I276 E287 K117 L157 K159 G164 G165 G166 I169 E201 Y203 I204 H209 Q233 I278 E289
BS03 MG B E274 E287 E276 E289
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:7kct, PDBe:7kct, PDBj:7kct
PDBsum7kct
PubMed33464881
UniProtD3DJ42|2OCS_HYDTT 2-oxoglutarate carboxylase small subunit (Gene Name=cfiB)

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