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X-ray crystallographic structure of a C70Q mycobacterium smegmatis N- arylamine acetyltransferase

Analyse X-ray crystallographic structure of a C70Q mycobacterium smegmatis N- arylamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1W5R
Type: protein
Length: 546 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arylamine N-acetyltransferase
EC: 2.3.1.5
UniProt: O86309
Pockets: 4 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Arylamine N-acetyltransferase (EC 2.3.1.5)	protein	273	33% helix, 27% strand	O86309

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	354	0.62	0.78	38	empty
2	320	0.58	0.77	34	empty
3	79	0.34	0.75	17	empty
4	60	0.30	0.75	13	empty

Interfaces

1 interface between chains.

A–B · 512 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

1W5R · X-ray crystallographic structure of a C70Q Mycobacterium smegmatis N- arylamine… · the same entry in another collection · chain A against A, TM-score 1.00
O86309 · AlphaFold monomer V2.0 prediction for arylamine N-acetyltransferase (O86309) · a predicted model of the same protein · 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 O86309
Elsewhere: RCSB PDB 1W5R · PDBe 1W5R · UniProt O86309

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