MolNFT v1 · #144221 · protein

Crystal structure of acetyl-CoA acetyltransferase from elizabethkingia anophelis NUHP1

6BN2: “Crystal structure of acetyl-CoA acetyltransferase from elizabethkingia anophelis NUHP1”. X-ray diffraction, 2 ligands (CA, CL), 1 pocket (best druggability 0.51). MolNFT v1 #144221 on GenesisL1: 3D structure, binding sites and…

PDB: 6BN2
Type: protein
Length: 393 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyl-CoA acetyltransferase
EC: 2.3.1.9
UniProt: A0A077EEP0
Ligands: CA, CL
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyl-CoA acetyltransferase (EC 2.3.1.9)	protein	393	40% helix, 22% strand	A0A077EEP0

Ligands and binding sites

CA · Calcium ion · metal · 3 copies · chains A
CL · Chloride ion · ion · chains A
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	91	0.51	0.82	17	empty

Modifications

Observed in the structure: 2 modified (acetylation).

Compared structures

6BN2 · Crystal structure of Acetyl-CoA acetyltransferase from Elizabethkingia anophelis NUHP1 · 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 A0A077EEP0
Elsewhere: RCSB PDB 6BN2 · PDBe 6BN2 · UniProt A0A077EEP0

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