Structure of PDB 3ufx Chain G

Receptor sequence

>3ufxG (length=369) Species: 271 (Thermus aquaticus)

MNLHEYQAKEILARYGVPVPPGKVAYTPEEAKRIAEEFGKRVVIKAQVHV
GGRGKAGGVKLADTPQEAYEKAQAILGMNIKGLTVKKVLVAEAVDIAKEY
YAGLILDRAKKRVVLMLSKEGGVDIEEVAAERPEAIHKFWIDPHKGFRPF
EAREMVKRAGLEGNLNKLAQVLVALYRAYEGVDASIAEINPLVVTTDGGI
VAADAKIVLDDNALFRHPDLAELREVEAEHPLEVEASNYGFAYVKLDGNI
GIIGNGAGLVMYTLDLVNRVGGKPANFLDIGGGAKADVVYNALKVVLKDP
DVKGVFINIFGGITRADEVAKGVIRALEEGLLTKPVVMRVAGTAEEEAKK
LLKPVYMYPTSIEAAKVTV

3D structure

• PDB: 3ufx Biochemical and structural characterization of the GTP-preferring succinyl-CoA synthetase from Thermus aquaticus.
• Chain: G
• Resolution: 2.35 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y101 E188
• Catalytic site (residue number reindexed from 1): Y101 E188
• 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	G	V43 K45 R53 A93 V94 I96 E99 D204	V43 K45 R53 A93 V94 I96 E99 D204
BS02	MN	G	N190 D204	N190 D204

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003824 catalytic activity
• GO:0004775 succinate-CoA ligase (ADP-forming) activity
• GO:0004776 succinate-CoA ligase (GDP-forming) activity
• 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:0005829 cytosol
• GO:0042709 succinate-CoA ligase complex

External links

• PDB: RCSB:3ufx, PDBe:3ufx, PDBj:3ufx
• PDBsum: 3ufx
• PubMed: 22751660
• UniProt: P25126|SUCC_THETH Succinate--CoA ligase [GDP-forming] subunit beta (Gene Name=sucC)