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The crystal structure of the outer membrane protein vcec from the bacterial pathogen vibrio cholerae at 1.8 resolution

Analyse The crystal structure of the outer membrane protein vcec from the bacterial… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YC9
Type: protein
Length: 411 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Multidrug resistance protein
UniProt: Q9KS51
Ligands: HG
Pockets: 4 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 68% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Multidrug resistance protein	protein	411	68% helix, 12% strand	Q9KS51

Ligands and binding sites

HG · Mercury (II) ion · metal · 2 copies · chains A
BOG · octyl beta-D-glucopyranoside · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	101	0.37	0.74	14	empty
2	60	0.37	0.78	14	empty
3	66	0.34	0.77	15	empty
4	73	0.31	0.73	14	empty

Compared structures

1YC9 · The crystal structure of the outer membrane protein VceC from the bacterial pathogen… · 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 Q9KS51
Elsewhere: RCSB PDB 1YC9 · PDBe 1YC9 · UniProt Q9KS51

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