Research workbench

Circularly permuted beta-lactamase from staphylococcus aureus PC1

Analyse Circularly permuted beta-lactamase from staphylococcus aureus PC1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ALQ
Type: protein
Length: 259 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CP254 beta-lactamase
EC: 3.5.2.6
UniProt: P00807
Ligands: SO4, CO3
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CP254 beta-lactamase (EC 3.5.2.6)	protein	259	43% helix, 19% strand	P00807

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A
CO3 · Carbonate ion · ion · 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	74	0.30	0.74	17	empty

Compared structures

1ALQ · Circularly permuted beta-lactamase from staphylococcus aureus PC1 · the same entry in another collection · chain A against A, TM-score 1.00
P00807 · AlphaFold monomer V2.0 prediction for beta-lactamase (P00807) · a predicted model of the same protein · chain A against A, TM-score 0.85

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 P00807
Elsewhere: RCSB PDB 1ALQ · PDBe 1ALQ · UniProt P00807

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