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X-ray crystal structure of oxa-24/40 K84D in complex with cefotaxime

Analyse X-ray crystal structure of oxa-24/40 K84D 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: 7RPG
Type: protein
Length: 244 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: Q8RLA6
Ligands: CEF, SO4
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	244	42% helix, 21% strand	Q8RLA6

Ligands and binding sites

CEF · CEFOTAXIME, C3' cleaved, open, bound form · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · 2 copies · 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	143	0.42	0.75	21	CEF

Modifications

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

Compared structures

7RPG · X-ray crystal structure of OXA-24/40 K84D 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 Q8RLA6
Elsewhere: RCSB PDB 7RPG · PDBe 7RPG · UniProt Q8RLA6

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