Research workbench

Bipd of burkholderia pseudomallei

Analyse Bipd of burkholderia pseudomallei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2J9T
Type: protein
Length: 504 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Membrane antigen
UniProt: Q63K37
Ligands: BO3
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 67% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Membrane antigen	protein	252	67% helix, 12% strand	Q63K37

Ligands and binding sites

BO3 · Boric acid · ion · 2 copies · chains A, B
FLC · Citrate anion · additive · chains A

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

Pockets

2 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	348	0.54	0.74	45	empty
2	69	0.31	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 474 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

2J9T · BipD of Burkholderia Pseudomallei · the same entry in another collection · chain A against A, TM-score 1.00
Q63K37 · AlphaFold monomer V2.0 prediction for translocator protein bipd (Q63K37) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q63K37
Elsewhere: RCSB PDB 2J9T · PDBe 2J9T · UniProt Q63K37

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