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Cryo-EM structure of ATP-bound PCAT1 in the outward-facing conformation

Analyse Cryo-EM structure of ATP-bound PCAT1 in the outward-facing conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7T54
Type: protein
Length: 1,416 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ABC-type bacteriocin transporter
UniProt: A3DCU1
Ligands: ATP
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · 1 distinct chain · 56% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	ABC-type bacteriocin transporter	protein	708	56% helix, 11% strand	A3DCU1

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B

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

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	794	0.87	0.90	110	ATP
2	860	0.80	0.83	87	empty
3	127	0.68	0.90	29	ATP
4	56	0.68	0.96	15	empty
5	579	0.68	0.78	63	empty

Interfaces

1 interface between chains.

A–B · 4922 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

7T54 · Cryo-EM structure of ATP-bound PCAT1 in the outward-facing 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 A3DCU1
Elsewhere: RCSB PDB 7T54 · PDBe 7T54 · UniProt A3DCU1

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