Research workbench

Ctx-M-9 S70G in complex with hydrolyzed piperacillin

Analyse Ctx-M-9 S70G in complex with hydrolyzed piperacillin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3Q1F
Type: protein
Length: 522 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: Q9L5C8
Ligands: YPP
Pockets: 2 · best druggability 0.39

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	262	44% helix, 19% strand	Q9L5C8
B	Beta-lactamase (EC 3.5.2.6)	protein	260	44% helix, 20% strand	Q9L5C8

Ligands and binding sites

YPP · Hydrolyzed piperacillin · ligand · 4 copies · chains A, B

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	103	0.39	0.76	21	YPP
2	96	0.36	0.75	22	YPP

Interfaces

1 interface between chains.

A–B · 71 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

3Q1F · CTX-M-9 S70G in complex with hydrolyzed piperacillin · the same entry in another collection · chain B against B, 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 Q9L5C8
Elsewhere: RCSB PDB 3Q1F · PDBe 3Q1F · UniProt Q9L5C8

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