MolNFT v1 · #187091 · protein

The role of an asp-asp pair in the structure, function and inhibition of ctx-M class a beta-lactamase

7S0V: “The role of an asp-asp pair in the structure, function and inhibition of ctx-M class a beta-lactamase”. X-ray diffraction, 1 ligand (J1X), 1 pocket (best druggability 0.37). MolNFT v1 #187091 on GenesisL1: 3D structure, binding…

PDB: 7S0V
Type: protein
Length: 262 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: Q9L5C7
Ligands: J1X
Pockets: 1 · best druggability 0.37

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	262	43% helix, 19% strand	Q9L5C7

Ligands and binding sites

J1X · 3-(1H-pyrazol-1-yl)-N-[3-(1H-tetrazol-5-yl)phenyl]-5-(trifluoromethyl)benzamide · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	95	0.37	0.76	19	J1X

Compared structures

7S0V · The role of an Asp-Asp pair in the structure, function and inhibition of CTX-M Class A… · 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 Q9L5C7
Elsewhere: RCSB PDB 7S0V · PDBe 7S0V · UniProt Q9L5C7

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