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Crystal structure of a class C beta-lactamase in complex with cefotaxime

Analyse Crystal structure of a class C beta-lactamase in complex with cefotaxime in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6K9T
Type: protein
Length: 358 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.459
Source: Klebsiella pneumoniae
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: Q9XB24
Ligands: CEF
Pockets: 2 · best druggability 0.58

Structure

x-ray diffraction · resolution 1.459 · 1 distinct chain · 40% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	358	40% helix, 24% strand	Q9XB24

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

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	312	0.58	0.77	43	CEF
2	90	0.33	0.73	22	empty

Modifications

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

Compared structures

6K9T · Crystal structure of a class C beta-lactamase in complex with cefotaxime · 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 Q9XB24
Elsewhere: RCSB PDB 6K9T · PDBe 6K9T · UniProt Q9XB24

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