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Crystal structure of Vibrio cholerae MATE transporter VcmN in the straight form

Analyse Crystal structure of Vibrio cholerae MATE transporter VcmN in the straight form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IDP
Type: protein
Length: 438 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.205
Source: Vibrio cholerae
Molecule: MATE family efflux transporter
UniProt: A0A2A1YWE9
Pockets: 4 · best druggability 0.82

Structure

x-ray diffraction · resolution 2.205 · 1 distinct chain · 88% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MATE family efflux transporter	protein	438	88% helix, 0% strand	A0A2A1YWE9

Ligands and binding sites

OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 19 copies · chains A

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

Pockets

4 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	1033	0.82	0.83	75	OLC
2	122	0.40	0.75	23	empty
3	82	0.39	0.77	12	OLC
4	68	0.34	0.76	16	empty

Compared structures

6IDP · Crystal structure of vibrio cholerae mate transporter vcmn in the straight form · 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 A0A2A1YWE9
Elsewhere: RCSB PDB 6IDP · PDBe 6IDP · UniProt A0A2A1YWE9

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