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Solution structure of the bacillus cereus metallo-beta-lactamase bcii in complex with R-thiomandelic acid

Analyse Solution structure of the bacillus cereus metallo-beta-lactamase bcii in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2M5D
Type: protein
Length: 227 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase 2
EC: 3.5.2.6
UniProt: P04190
Ligands: RTD, ZN
Pockets: 1 · best druggability 0.42

Structure

solution nmr · 1 distinct chain · 25% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase 2 (EC 3.5.2.6)	protein	227	25% helix, 19% strand	P04190

Ligands and binding sites

RTD · (2R)-phenyl(sulfanyl)ethanoic acid · ligand · chains A
ZN · Zinc ion · metal · 2 copies · 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	142	0.42	0.74	21	RTD

Compared structures

2M5D · Solution Structure of the Bacillus cereus Metallo-Beta-Lactamase BcII in Complex with… · 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 0.95

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 2M5D · PDBe 2M5D · UniProt P04190

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