Structure of PDB 2fpg Chain A

Receptor sequence
>2fpgA (length=305) Species: 9823 (Sus scrofa) [Search protein sequence]
SYTASRKHLYVDKNTKVICQGFTGKQGTFHSQQALEYGTNLVGGTTPGKG
GKTHLGLPVFNTVKEAKEQTGATASVIYVPPPFAAAAINEAIDAEVPLVV
CITEGIPQQDMVRVKHRLLRQGKTRLIGPNCPGVINPGECKIGIMPGHIH
KKGRIGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFTDCLE
IFLNDPATEGIILIGEIGGNAEENAAEFLKQHNSGPKSKPVVSFIAGLTA
PPGRRMGHAGAIIAGGKGGAKEKITALQSAGVVVSMSPAQLGTTIYKEFE
KRKML
3D structure
PDB2fpg Interactions of GTP with the ATP-grasp Domain of GTP-specific Succinyl-CoA Synthetase
ChainA
Resolution2.96 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E217 H259
Catalytic site (residue number reindexed from 1) E216 H258
Enzyme Commision number 6.2.1.4: succinate--CoA ligase (GDP-forming).
6.2.1.5: succinate--CoA ligase (ADP-forming).
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 PO4 A S162 G163 T164 H259 S161 G162 T163 H258
Gene Ontology
Molecular Function
GO:0003824 catalytic activity

View graph for
Molecular Function
External links
PDB RCSB:2fpg, PDBe:2fpg, PDBj:2fpg
PDBsum2fpg
PubMed16481318
UniProtO19069|SUCA_PIG Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (Gene Name=SUCLG1)

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