Structure of PDB 3ufx Chain E

Receptor sequence
>3ufxE (length=373) Species: 271 (Thermus aquaticus) [Search protein sequence]
MNLHEYQAKEILARYGVPVPPGKVAYTPEEAKRIAEEFGKRVVIKAQVHV
GGRGKAGGVKLADTPQEAYEKAQAILGMNIKGLTVKKVLVAEAVDIAKEY
YAGLILDRAKKRVVLMLSKEGGVDIEEVAAERPEAIHKFWIDPHKGFRPF
EAREMVKRAGLEGNLNKLAQVLVALYRAYEGVDASIAEINPLVVTTDGGI
VAADAKIVLDDNALFRHPDLAELREVEAEHPLEVEASNYGFAYVKLDGNI
GIIGNGAGLVMYTLDLVNRVGGKPANFLDIGGGAKADVVYNALKVVLKDP
DVKGVFINIFGGITRADEVAKGVIRALEEGLLTKPVVMRVAGTAEEEAKK
LLEGKPVYMYPTSIEAAKVTVAM
3D structure
PDB3ufx Biochemical and structural characterization of the GTP-preferring succinyl-CoA synthetase from Thermus aquaticus.
ChainE
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 E V43 K45 G52 R53 A93 V94 I96 E99 D204 V43 K45 G52 R53 A93 V94 I96 E99 D204
BS02 MN E 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ufx, PDBe:3ufx, PDBj:3ufx
PDBsum3ufx
PubMed22751660
UniProtP25126|SUCC_THETH Succinate--CoA ligase [GDP-forming] subunit beta (Gene Name=sucC)

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