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Crystal structure of the class a beta-lactamase from mycobacterium fortuitum

Analyse Crystal structure of the class a beta-lactamase from mycobacterium fortuitum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CC1
Type: protein
Length: 262 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: Q59517
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	262	45% helix, 19% strand	Q59517

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	81	0.35	0.76	21	empty

Compared structures

2CC1 · Crystal structure of the class A beta-lactamase from Mycobacterium fortuitum · the same entry in another collection · chain A against A, TM-score 1.00
Q59517 · AlphaFold monomer V2.0 prediction for beta-lactamase (Q59517) · 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 Q59517
Elsewhere: RCSB PDB 2CC1 · PDBe 2CC1 · UniProt Q59517

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