Research workbench

Camp-binding acyltransferase from mycobacterium smegmatis, mutant R95K

Analyse Camp-binding acyltransferase from mycobacterium smegmatis, mutant R95K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ORF
Type: protein
Length: 319 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyltransferase pat
EC: 2.3.1.-
UniProt: A0R3F9
Ligands: CL
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyltransferase pat (EC 2.3.1.-)	protein	319	34% helix, 26% strand	A0R3F9

Ligands and binding sites

CL · Chloride ion · ion · 3 copies · 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	320	0.71	0.84	51	empty
2	108	0.42	0.77	24	empty
3	72	0.35	0.76	18	empty

Compared structures

4ORF · cAMP-binding acyltransferase from Mycobacterium smegmatis, mutant R95K · the same entry in another collection · chain A against A, TM-score 1.00
A0R3F9 · AlphaFold monomer V2.0 prediction for acetyltransferase pat (A0R3F9) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 A0R3F9
Elsewhere: RCSB PDB 4ORF · PDBe 4ORF · UniProt A0R3F9

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