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Crystal structure of ctx-M-14 S70G/N106S/D240G beta-lactamase in complex with hydrolyzed cefotaxime

Analyse Crystal structure of ctx-M-14 S70G/N106S/D240G beta-lactamase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6CYU
Type: protein
Length: 261 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: CE4
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	261	43% helix, 20% strand	Q9L5C7

Ligands and binding sites

CE4 · (2R)-2-[(R)-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}(carboxy)methyl]-5-methylidene-5,6-dihydro -2H-1,3-thiazine-4-carboxylic acid · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	128	0.43	0.77	23	CE4
2	54	0.34	0.78	18	empty

Compared structures

6CYU · Crystal structure of CTX-M-14 S70G/N106S/D240G beta-lactamase in complex with hydrolyzed… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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Every structure of UniProt Q9L5C7
Elsewhere: RCSB PDB 6CYU · PDBe 6CYU · UniProt Q9L5C7

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