Research workbench

Ctx-M9 mutant L48A

Analyse Ctx-M9 mutant L48A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5KMT
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: K, PO4
Pockets: 5 · best druggability 0.51

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Beta-lactamase (EC 3.5.2.6)	protein	261	43% helix, 20% strand	Q9L5C8

Ligands and binding sites

K · Potassium ion · metal · 4 copies · chains A, B
PO4 · Phosphate ion · ion · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	238	0.51	0.76	22	empty
2	232	0.49	0.75	24	empty
3	52	0.42	0.82	19	empty
4	90	0.34	0.75	21	PO4, K
5	72	0.34	0.76	18	PO4

Interfaces

1 interface between chains.

A–B · 160 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5KMT · CTX-M9 mutant L48A · 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 Q9L5C8
Elsewhere: RCSB PDB 5KMT · PDBe 5KMT · UniProt Q9L5C8

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