Structure of PDB 7jmk Chain B

Receptor sequence
>7jmkB (length=379) Species: 9823 (Sus scrofa) [Search protein sequence]
MNLQEYQSKKLMSDNGVKVQRFFVADTANELNAKEIVLKAQILAGGRGLK
GGVHLTKDPEVVGQLAKQMIGYNLATKQTPKEGVKVNKVMVAEALDISRE
TYLAILMDRSCNGPVLVGSPQGGVDIEEVAASNPELIFKEQIDIIEGIKD
SQAQRMAENLGFLGPLQNQAADQIKKLYNLFLKIDATQVEVNPFGETPEG
QVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLDG
NIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKESQVYQAFKLLTA
DPKVEAILVNIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVHEA
QNILTNSGLPITSAVDLEDAAKKAVASVT
3D structure
PDB7jmk Second distinct conformation of the phosphohistidine loop in succinyl-CoA synthetase
ChainB
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) Y116 E204
Catalytic site (residue number reindexed from 1) Y102 E190
Enzyme Commision number 6.2.1.4: succinate--CoA ligase (GDP-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 GDP B K46 R54 V67 L69 L109 I111 E114 V138 K39 R47 V53 L55 L95 I97 E100 V124
BS02 MG B N206 D220 N192 D206
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004775 succinate-CoA ligase (ADP-forming) activity
GO:0004776 succinate-CoA ligase (GDP-forming) activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0005525 GTP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006099 tricarboxylic acid cycle
GO:0006104 succinyl-CoA metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0042709 succinate-CoA ligase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7jmk, PDBe:7jmk, PDBj:7jmk
PDBsum7jmk
PubMed
UniProtP53590|SUCB2_PIG Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (Fragment) (Gene Name=SUCLG2)

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