MolNFT v1 · #178586 · protein

GTP-specific succinyl-CoA synthetase complexed with mg-GDP, phosphohistidine loop pointing towards nucleotide binding site

7JFP: “GTP-specific succinyl-CoA synthetase complexed with mg-GDP, phosphohistidine loop pointing towards nucleotide…”. X-ray diffraction, 2 ligands (GDP, MG). MolNFT v1 #178586 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7JFP
Type: protein
Length: 696 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: O19069, P53590
Ligands: GDP, MG

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	303	—	O19069
B	—	protein	393	—	P53590

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains B
MG · Magnesium ion · metal · chains A, B
GOL · Glycerol · additive · 3 copies · chains A, B

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

Compared structures

7JFP · GTP-specific succinyl-CoA synthetase complexed with Mg-GDP, phosphohistidine loop… · the same entry in another collection · chain A against A, 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 A against A, TM-score 0.96
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 0.96

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 7JFP · PDBe 7JFP · UniProt O19069 · UniProt P53590

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