MolNFT v1 · #171358 · protein

Acylenzyme complex of ceftazidime bound to deacylation mutant kpc-4 (E166Q)

6Z25 · Beta-lactamase: “Acylenzyme complex of ceftazidime bound to deacylation mutant kpc-4 (E166Q)”. X-ray diffraction, 2 ligands (CAZ, SO4), 1 pocket (best druggability 0.62). MolNFT v1 #171358 on GenesisL1: 3D structure, binding sites…

PDB: 6Z25
Type: protein
Length: 270 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: B1PL86
Ligands: CAZ, SO4
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	270	39% helix, 17% strand	B1PL86

Ligands and binding sites

CAZ · Acylated ceftazidime · ligand · chains A
SO4 · Sulfate ion · ion · 5 copies · chains A
GOL · Glycerol · additive · 4 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	217	0.62	0.82	37	CAZ

Modifications

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

Compared structures

6Z25 · Acylenzyme complex of ceftazidime bound to deacylation mutant KPC-4 (E166Q) · 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 B1PL86
Elsewhere: RCSB PDB 6Z25 · PDBe 6Z25 · UniProt B1PL86

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