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Helical structure of the toxin maka from vibrio cholera

Analyse Helical structure of the toxin maka from vibrio cholera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7P3R
Type: protein
Length: 1,338 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Maka tetramer
UniProt: Q9KL64
Pockets: 15 · best druggability 0.81

Structure

electron microscopy · 2 distinct chains · 84% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Maka tetramer	protein	328	84% helix, 0% strand	Q9KL64
B, D	Maka tetramer	protein	341	84% helix, 0% strand	Q9KL64

Pockets

15 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1120	0.81	0.82	96	empty
2	704	0.80	0.84	111	empty
3	668	0.77	0.83	120	empty
4	462	0.75	0.84	76	empty
5	403	0.73	0.83	72	empty

Interfaces

6 interfaces between chains.

A–B · 1707 Å² buried · 3 hydrogen bonds · protein-protein
C–D · 1534 Å² buried · 5 hydrogen bonds · protein-protein
A–C · 407 Å² buried · 1 hydrogen bond · protein-protein
B–D · 383 Å² buried · 1 hydrogen bond · protein-protein
A–D · 146 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

7P3R · Helical structure of the toxin MakA from Vibrio cholera · 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 Q9KL64
Elsewhere: RCSB PDB 7P3R · PDBe 7P3R · UniProt Q9KL64

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