MolNFT v1 · #51702 · protein

The structure of mycobacterium marinum arylamine N-acetyltransferase in complex with CoA

2VFC: “The structure of mycobacterium marinum arylamine N-acetyltransferase in complex with CoA”. X-ray diffraction, 1 ligand (COA), 3 pockets (best druggability 0.70). MolNFT v1 #51702 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 2VFC
Type: protein
Length: 543 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arylamine N-acetyltransferase
EC: 2.3.1.5
Ligands: COA
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Arylamine N-acetyltransferase (EC 2.3.1.5)	protein	272	33% helix, 27% strand	—
B	Arylamine N-acetyltransferase (EC 2.3.1.5)	protein	271	34% helix, 25% strand	—

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

3 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	609	0.70	0.78	58	COA
2	572	0.68	0.77	51	COA
3	383	0.67	0.81	45	empty

Interfaces

1 interface between chains.

A–B · 748 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

2VFC · The structure of Mycobacterium marinum arylamine N-acetyltransferase in complex with CoA · 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
Elsewhere: RCSB PDB 2VFC · PDBe 2VFC

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