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Shv-1 class a beta-lactamase complexed with penem WAY185229

Analyse Shv-1 class a beta-lactamase complexed with penem WAY185229 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Q2P
Type: protein
Length: 265 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase shv-1
EC: 3.5.2.6
UniProt: P14557
Ligands: MA4, WY2
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase shv-1 (EC 3.5.2.6)	protein	265	46% helix, 17% strand	P14557

Ligands and binding sites

MA4 · Cyclohexyl-hexyl-beta-D-maltoside · ligand · 2 copies · chains A
WY2 · (6,7-dihydro-5H-cyclopenta[d]imidazo[2,1-b]thiazol-2-yl]-4,7-dihydro[1,4]thiazepine-3,6-dicarboxylic acid · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	205	0.67	0.85	24	MA4

Modifications

Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).

Compared structures

1Q2P · SHV-1 class A beta-lactamase complexed with penem WAY185229 · the same entry in another collection · 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 P14557
Elsewhere: RCSB PDB 1Q2P · PDBe 1Q2P · UniProt P14557

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