Research workbench

GTP-specific succinyl-CoA synthetase complexed with mg-gmppcp

Analyse GTP-specific succinyl-CoA synthetase complexed with mg-gmppcp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7JJ0
Type: protein
Length: 1,368 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: O19069, P53590
Ligands: GCP, MG

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	296	—	O19069
B	—	protein	393	—	P53590
C	—	protein	297	—	O19069
D	—	protein	382	—	P53590

Ligands and binding sites

GCP · Phosphomethylphosphonic acid guanylate ester · ligand · chains A, B
MG · Magnesium ion · metal · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

7JJ0 · GTP-specific succinyl-CoA synthetase complexed with Mg-GMPPCP · the same entry in another collection · chain D against D, TM-score 1.00
O19069 · AlphaFold monomer V2.0 prediction for succinate--CoA ligase [ADP/GDP- forming] subunit… · a predicted model of the same protein · chain C against A, TM-score 0.98
P53590 · AlphaFold monomer V2.0 prediction for succinate--CoA ligase [GDP- forming] subunit beta… · a predicted model of the same protein · chain B against A, TM-score 0.95

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O19069
Every structure of UniProt P53590
Elsewhere: RCSB PDB 7JJ0 · PDBe 7JJ0 · UniProt O19069 · UniProt P53590

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