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Structure of XECO2 acetyltransferase domain

Analyse Structure of XECO2 acetyltransferase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5N1U
Type: protein
Length: 340 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: XECO2
UniProt: A8QZK6
Ligands: COA
Pockets: 6 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	XECO2	protein	170	27% helix, 29% strand	A8QZK6
B	XECO2	protein	170	27% helix, 29% strand	A8QZK6

Ligands and binding sites

COA · Coenzyme A · ligand · 2 copies · chains A, B

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	387	0.66	0.79	45	COA
2	349	0.61	0.77	43	COA
3	65	0.51	0.86	18	empty
4	122	0.49	0.79	20	empty
5	110	0.47	0.79	17	empty

Interfaces

1 interface between chains.

A–B · 720 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

5N1U · Structure of xEco2 acetyltransferase domain · 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 A8QZK6
Elsewhere: RCSB PDB 5N1U · PDBe 5N1U · UniProt A8QZK6

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