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Structure of ESCO2 acetyltransferase in complex with CoA

Analyse Structure of ESCO2 acetyltransferase in complex with CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SP0
Type: protein
Length: 197 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acetyltransferase ESCO2
EC: 2.3.1.-
UniProt: Q8CIB9
Ligands: COA, ZN
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acetyltransferase ESCO2 (EC 2.3.1.-)	protein	197	31% helix, 30% strand	Q8CIB9

Ligands and binding sites

COA · Coenzyme A · ligand · chains A
ZN · Zinc ion · metal · chains A

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

Pockets

3 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	250	0.65	0.82	31	COA
2	140	0.48	0.78	20	empty
3	64	0.35	0.77	13	empty

Compared structures

6SP0 · Structure of Esco2 acetyltransferase in complex with CoA · the same entry in another collection · chain A against A, TM-score 1.00
Q8CIB9 · AlphaFold monomer V2.0 prediction for N-acetyltransferase ESCO2 (Q8CIB9) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q8CIB9
Elsewhere: RCSB PDB 6SP0 · PDBe 6SP0 · UniProt Q8CIB9

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