MolNFT v1 · #179350 · protein

Crystal structure of ctx-M-14 E166A/K234R beta-lactamase in complex with hydrolyzed cefotaxime

7K2W: “Crystal structure of ctx-M-14 E166A/K234R beta-lactamase in complex with hydrolyzed cefotaxime”. X-ray diffraction, 1 ligand (CEF), 1 pocket (best druggability 0.34). MolNFT v1 #179350 on GenesisL1: 3D structure, binding sites and…

PDB: 7K2W
Type: protein
Length: 260 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: A0A2H4FY00
Ligands: CEF
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	260	44% helix, 20% strand	A0A2H4FY00

Ligands and binding sites

CEF · CEFOTAXIME, C3' cleaved, open, bound form · 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	78	0.34	0.76	21	CEF

Modifications

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

Compared structures

7K2W · Crystal structure of CTX-M-14 E166A/K234R Beta-lactamase in complex with hydrolyzed… · 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 A0A2H4FY00
Elsewhere: RCSB PDB 7K2W · PDBe 7K2W · UniProt A0A2H4FY00

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