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Structure of ctx-M-15 bound to rpx-7063 at 1.5A

Analyse Structure of ctx-M-15 bound to rpx-7063 at 1.5A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7TI0
Type: protein
Length: 260 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: Q2PUH3
Ligands: ZXQ, SO4, CL
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	260	44% helix, 19% strand	Q2PUH3

Ligands and binding sites

ZXQ · {(3R,7S)-2-hydroxy-3-[2-(thiophen-2-yl)acetamido]-2,3, 4,7-tetrahydro-1,2-oxaborepin-7-yl}acetic acid · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
CL · Chloride ion · ion · chains A
EDO · 1,2-ethanediol · additive · 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	71	0.32	0.76	19	ZXQ

Modifications

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

Compared structures

7TI0 · Structure of CTX-M-15 bound to RPX-7063 at 1.5A · 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 Q2PUH3
Elsewhere: RCSB PDB 7TI0 · PDBe 7TI0 · UniProt Q2PUH3

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