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The crystal structure of an ABC transporter from rhodopseudomonas palustris CGA009

Analyse The crystal structure of an ABC transporter from rhodopseudomonas palustris… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3RPW
Type: protein
Length: 333 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ABC transporter
UniProt: Q6N0W2
Ligands: URE
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ABC transporter	protein	333	46% helix, 20% strand	Q6N0W2

Ligands and binding sites

URE · Urea · ligand · chains A
FMT · Formic acid · additive · 10 copies · chains A
GOL · Glycerol · additive · 3 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	153	0.72	0.91	39	GOL
2	120	0.42	0.76	20	FMT
3	91	0.37	0.75	21	FMT
4	76	0.35	0.76	13	empty

Modifications

Observed in the structure: 9 modified, 1 disulfide (engineered, disulfide).

Compared structures

3RPW · The crystal structure of an ABC transporter from Rhodopseudomonas palustris CGA009 · 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 Q6N0W2
Elsewhere: RCSB PDB 3RPW · PDBe 3RPW · UniProt Q6N0W2

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