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ABC-transporter choline binding protein in unliganded semi-closed conformation

Analyse ABC-transporter choline binding protein in unliganded semi-closed conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2REJ
Type: protein
Length: 576 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative glycine betaine ABC transporter protein
UniProt: Q92N37
Pockets: 10 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative glycine betaine ABC transporter protein	protein	288	33% helix, 19% strand	Q92N37

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	181	0.80	0.94	35	empty
2	175	0.78	0.93	33	empty
3	109	0.74	0.94	24	empty
4	128	0.74	0.93	25	empty
5	166	0.72	0.89	36	empty

Interfaces

1 interface between chains.

A–B · 70 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2REJ · ABC-transporter choline binding protein in unliganded semi-closed conformation · 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 Q92N37
Elsewhere: RCSB PDB 2REJ · PDBe 2REJ · UniProt Q92N37

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