Research workbench

Tem-1 class-a beta-lactamase L201P mutant apo structure

Analyse Tem-1 class-a beta-lactamase L201P mutant apo structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CMZ
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase tem
EC: 3.5.2.6
UniProt: P62593
Ligands: PO4
Pockets: 2 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase tem (EC 3.5.2.6)	protein	263	43% helix, 17% strand	P62593

Ligands and binding sites

PO4 · Phosphate ion · ion · 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	75	0.34	0.76	15	empty
2	59	0.33	0.77	18	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3CMZ · TEM-1 Class-A beta-lactamase L201P mutant apo structure · the same entry in another collection · chain A against A, TM-score 1.00
P62593 · AlphaFold monomer V2.0 prediction for beta-lactamase tem (P62593) · 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 P62593
Elsewhere: RCSB PDB 3CMZ · PDBe 3CMZ · UniProt P62593

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