MolNFT v1 · #69514 · protein

Structure and mechanism of the heavy metal transporter cusa

3KSS · Cation efflux system protein cusa: “Structure and mechanism of the heavy metal transporter cusa”. X-ray diffraction, 1 ligand (CU1), 18 pockets (best druggability 0.82). MolNFT v1 #69514 on GenesisL1: 3D structure, binding sites and…

PDB: 3KSS
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: 18 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cation efflux system protein cusa	protein	1015	52% helix, 17% strand	P38054

Ligands and binding sites

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

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

Pockets

18 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	994	0.82	0.83	104	empty
2	976	0.81	0.82	97	empty
3	73	0.76	0.99	25	empty
4	66	0.70	0.96	23	empty
5	68	0.70	0.95	23	empty

Compared structures

3KSS · 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 0.94

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 3KSS · PDBe 3KSS · UniProt P38054

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