Structure of PDB 2fpg Chain B

Receptor sequence

>2fpgB (length=393) Species: 9823 (Sus scrofa)

MNLQEYQSKKLMSDNGVKVQRFFVADTANEALEAAKRLNAKEIVLKAQIL
AGGRGKGVFSSGLKGGVHLTKDPEVVGQLAKQMIGYNLATKQTPKEGVKV
NKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEVAASNPEL
IFKEQIDIIEGIKDSQAQRMAENLGFLGPLQNQAADQIKKLYNLFLKIDA
TQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIEN
EAAKYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGV
KESQVYQAFKLLTADPKVEAILVNIFGGIVNCAIIANGITKACRELELKV
PLVVRLEGTNVHEAQNILTNSGLPITSAVDLEDAAKKAVASVT

3D structure

• PDB: 2fpg Interactions of GTP with the ATP-grasp Domain of GTP-specific Succinyl-CoA Synthetase
• Chain: B
• Resolution: 2.96 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y116 E204
• Catalytic site (residue number reindexed from 1): Y116 E204
• 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	Q20 G52 G53 R54 G55 V67 L69 L109	Q20 G52 G53 R54 G55 V67 L69 L109

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

External links

• PDB: RCSB:2fpg, PDBe:2fpg, PDBj:2fpg
• PDBsum: 2fpg
• PubMed: 16481318
• UniProt: P53590|SUCB2_PIG Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (Fragment) (Gene Name=SUCLG2)