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Structure of ctx-M-15 E166Q mutant crystallised in the presence of tazobactam (AAI101)

Analyse Structure of ctx-M-15 E166Q mutant crystallised in the presence of tazobactam… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BDR
Type: protein
Length: 259 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: W1EPV7
Ligands: NA, SO4, CL
Pockets: 1 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	259	43% helix, 19% strand	W1EPV7

Ligands and binding sites

NA · Sodium ion · metal · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
CL · Chloride ion · ion · 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	123	0.39	0.75	26	empty

Modifications

Observed in the structure: 1 d-amino (D-amino acid).

Compared structures

7BDR · Structure of CTX-M-15 E166Q mutant crystallised in the presence of tazobactam (AAI101) · 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 W1EPV7
Elsewhere: RCSB PDB 7BDR · PDBe 7BDR · UniProt W1EPV7

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