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Zn-dependent 5/B/6 metallo-beta-lactamase from bacillus cereus

Analyse Zn-dependent 5/B/6 metallo-beta-lactamase from bacillus cereus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6DJA
Type: protein
Length: 222 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Metallo-beta-lactamase type 2
EC: 3.5.2.6
UniProt: P14488
Ligands: ZN
Pockets: 2 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Metallo-beta-lactamase type 2 (EC 3.5.2.6)	protein	222	25% helix, 33% strand	P14488

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	63	0.29	0.74	17	ZN
2	59	0.27	0.73	19	empty

Compared structures

6DJA · Zn-dependent 5/B/6 metallo-beta-lactamase from bacillus cereus · the same entry in another collection · chain A against A, TM-score 1.00
P14488 · AlphaFold monomer V2.0 prediction for metallo-beta-lactamase type 2 (P14488) · 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 P14488
Elsewhere: RCSB PDB 6DJA · PDBe 6DJA · UniProt P14488

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