MolNFT v2 · #221678 · protein

Crystal Structure of Acetyl-coenzyme A synthetase from Leishmania infantum (CoA and AMP bound)

8U2T: “Crystal Structure of Acetyl-coenzyme A synthetase from Leishmania infantum (CoA and AMP bound)”. X-ray diffraction at 1.65, 4 ligands (AMP, COA, SO4), 5 pockets (best druggability 0.81). MolNFT v2 #221678 on GenesisL1: 3D structure…

PDB: 8U2T
Type: protein
Length: 661 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.65
Source: Leishmania infantum
Molecule: Acetyl-coenzyme A synthetase
UniProt: A4I093
Ligands: AMP, COA, SO4, CL
Pockets: 5 · best druggability 0.81

Structure

x-ray diffraction · resolution 1.65 · 1 distinct chain · 34% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyl-coenzyme A synthetase	protein	661	34% helix, 25% strand	A4I093

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · chains A
COA · Coenzyme A · ligand · chains A
SO4 · Sulfate ion · ion · 5 copies · chains A
CL · Chloride ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1045	0.81	0.82	104	SO4, AMP, COA
2	75	0.45	0.82	22	CL
3	94	0.42	0.78	16	empty
4	87	0.37	0.75	14	empty
5	75	0.32	0.74	18	empty

Modifications

Observed in the structure: 1 modified (oxidation).

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 A4I093
Elsewhere: RCSB PDB 8U2T · PDBe 8U2T · UniProt A4I093

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