MolNFT v1 · #20917 · protein

Crystal structure of the monomeric acetyl-CoA synthase from carboxydothermus hydrogenoformans

1RU3: “Crystal structure of the monomeric acetyl-CoA synthase from carboxydothermus hydrogenoformans”. X-ray diffraction, 2 ligands (SF4, NI), 6 pockets (best druggability 0.75). MolNFT v1 #20917 on GenesisL1: 3D structure, binding sites…

PDB: 1RU3
Type: protein
Length: 728 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyl-CoA synthase
UniProt: P83789
Ligands: SF4, NI
Pockets: 6 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyl-CoA synthase	protein	728	40% helix, 14% strand	P83789

Ligands and binding sites

SF4 · Iron/sulfur cluster · ligand · chains A
NI · Nickel (II) ion · metal · 2 copies · chains A
GOL · Glycerol · additive · 12 copies · chains A

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	103	0.75	0.95	34	empty
2	955	0.70	0.74	72	SF4, GOL
3	574	0.68	0.78	41	empty
4	223	0.48	0.74	25	empty
5	79	0.33	0.74	19	empty

Compared structures

1RU3 · Crystal Structure of the monomeric acetyl-CoA synthase from Carboxydothermus… · the same entry in another collection · chain A against A, TM-score 1.00

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 P83789
Elsewhere: RCSB PDB 1RU3 · PDBe 1RU3 · UniProt P83789

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