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Structure and mechanism of the heavy metal transporter cusa

Analyse Structure and mechanism of the heavy metal transporter cusa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KSO
Type: protein
Length: 1,014 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cation efflux system protein cusa
UniProt: P38054
Ligands: AG
Pockets: 20 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cation efflux system protein cusa	protein	1014	47% helix, 15% strand	P38054

Ligands and binding sites

AG · Silver ion · metal · chains A

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

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	924	0.82	0.83	110	empty
2	126	0.79	0.97	36	empty
3	804	0.79	0.82	78	empty
4	501	0.75	0.83	61	empty
5	65	0.74	0.99	19	empty

Compared structures

3KSO · Structure and Mechanism of the Heavy Metal Transporter 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 0.93

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 3KSO · PDBe 3KSO · UniProt P38054

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