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Ctx-M-14 N106S/D240G mutant

Analyse Ctx-M-14 N106S/D240G mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6CYN
Type: protein
Length: 2,087 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: Q9L5C7
Pockets: 20 · best druggability 0.80

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G	Beta-lactamase (EC 3.5.2.6)	protein	261	44% helix, 20% strand	Q9L5C7
H	Beta-lactamase (EC 3.5.2.6)	protein	260	44% helix, 20% strand	Q9L5C7

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1150	0.80	0.81	103	empty
2	939	0.78	0.81	87	empty
3	890	0.74	0.78	70	empty
4	780	0.73	0.78	68	empty
5	1146	0.69	0.74	112	empty

Interfaces

17 interfaces between chains.

G–H · 302 Å² buried · 4 hydrogen bonds · protein-protein
C–D · 298 Å² buried · 4 hydrogen bonds · protein-protein
E–F · 295 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 292 Å² buried · 7 hydrogen bonds · protein-protein
E–H · 272 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6CYN · CTX-M-14 N106S/D240G mutant · 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 Q9L5C7
Elsewhere: RCSB PDB 6CYN · PDBe 6CYN · UniProt Q9L5C7

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