MolNFT v1 · #58721 · protein

Metallo beta-lactamase II from bacillus cereus 569/H/9 at pH 6.0, monoclinic crystal form

3BC2: “Metallo beta-lactamase II from bacillus cereus 569/H/9 at pH 6.0, monoclinic crystal form”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.38). MolNFT v1 #58721 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 3BC2
Type: protein
Length: 215 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Metallo beta-lactamase II
EC: 3.5.2.6
UniProt: P04190
Ligands: ZN
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Metallo beta-lactamase II (EC 3.5.2.6)	protein	215	27% helix, 30% strand	P04190

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

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	101	0.38	0.75	21	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

3BC2 · Metallo beta-lactamase II from bacillus cereus 569/H/9 at pH 6.0, monoclinic crystal form · the same entry in another collection · chain A against A, TM-score 1.00
P04190 · AlphaFold monomer V2.0 prediction for metallo-beta-lactamase type 2 (P04190) · 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 P04190
Elsewhere: RCSB PDB 3BC2 · PDBe 3BC2 · UniProt P04190

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