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Crystal structure of the peptidase-containing ABC transporter PCAT1

Analyse Crystal structure of the peptidase-containing ABC transporter PCAT1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4RY2
Type: protein
Length: 1,400 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ABC-type bacteriocin transporter
EC: 3.4.22.-
UniProt: A3DCU1
Pockets: 20 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 60% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ABC-type bacteriocin transporter (EC 3.4.22.-)	protein	701	60% helix, 11% strand	A3DCU1
B	ABC-type bacteriocin transporter (EC 3.4.22.-)	protein	699	59% helix, 12% strand	A3DCU1

Pockets

20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	856	0.82	0.84	106	empty
2	118	0.76	0.95	25	empty
3	975	0.75	0.78	92	empty
4	825	0.70	0.75	84	empty
5	582	0.69	0.78	47	empty

Interfaces

1 interface between chains.

A–B · 5445 Å² buried · 26 hydrogen bonds · protein-protein

Compared structures

4RY2 · Crystal structure of the peptidase-containing ABC transporter PCAT1 · 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 A3DCU1
Elsewhere: RCSB PDB 4RY2 · PDBe 4RY2 · UniProt A3DCU1

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