MolNFT v1 · #182307 · protein

Crystal structure of acetyl-coenzyme a synthetase from legionella pneumophila philadelphia 1 in complex with ethyl-AMP

7MMZ: “Crystal structure of acetyl-coenzyme a synthetase from legionella pneumophila philadelphia 1 in complex with…”. X-ray diffraction, 1 ligand (WTA), 2 pockets (best druggability 0.82). MolNFT v1 #182307 on GenesisL1: 3D structure…

PDB: 7MMZ
Type: protein
Length: 559 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyl-coenzyme a synthetase
EC: 6.2.1.1
UniProt: Q5ZZ84
Ligands: WTA
Pockets: 2 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyl-coenzyme a synthetase (EC 6.2.1.1)	protein	559	32% helix, 27% strand	Q5ZZ84

Ligands and binding sites

WTA · 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine · ligand · chains A
EDO · 1,2-ethanediol · additive · chains A

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

Pockets

2 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	889	0.82	0.84	94	WTA, EDO
2	71	0.49	0.84	22	empty

Compared structures

7MMZ · Crystal Structure of Acetyl-coenzyme A synthetase from Legionella pneumophila… · 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 Q5ZZ84
Elsewhere: RCSB PDB 7MMZ · PDBe 7MMZ · UniProt Q5ZZ84

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