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Crystal structure of CU(I)CUSA

Analyse Crystal structure of CU(I)CUSA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3K0I
Type: protein
Length: 1,015 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cation efflux system protein cusa
UniProt: P38054
Ligands: CU1
Pockets: 19 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cation efflux system protein cusa	protein	1015	51% helix, 18% strand	P38054

Ligands and binding sites

CU1 · Copper (I) ion · metal · 2 copies · chains A

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

Pockets

19 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	772	0.78	0.81	77	empty
2	844	0.78	0.81	88	empty
3	526	0.77	0.84	51	empty
4	68	0.72	0.96	21	empty
5	179	0.65	0.85	29	empty

Compared structures

3K0I · Crystal structure of Cu(I)CusA · the same entry in another collection · chain A against A, TM-score 1.00
P38054 · AlphaFold monomer V2.0 prediction for cation efflux system protein cusa (P38054) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P38054
Elsewhere: RCSB PDB 3K0I · PDBe 3K0I · UniProt P38054

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