MolNFT v1 · #187521 · protein

Consensus structure of ATP7B

7SI3 · P-type cu(+) transporter: “Consensus structure of ATP7B”. Electron microscopy, 2 ligands (ALF, MG), 11 pockets (best druggability 0.75). MolNFT v1 #187521 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7SI3
Type: protein
Length: 872 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P-type cu(+) transporter
EC: 7.2.2.8
UniProt: A0A6I8R0A5
Ligands: ALF, MG
Pockets: 11 · best druggability 0.75

Structure

electron microscopy · 1 distinct chain · 50% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P-type cu(+) transporter (EC 7.2.2.8)	protein	872	50% helix, 18% strand	A0A6I8R0A5

Ligands and binding sites

ALF · Tetrafluoroaluminate ion · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	999	0.75	0.78	94	empty
2	633	0.74	0.80	71	empty
3	369	0.61	0.78	48	empty
4	77	0.56	0.87	20	empty
5	202	0.51	0.77	32	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7SI3 · Consensus structure of ATP7B · 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 A0A6I8R0A5
Elsewhere: RCSB PDB 7SI3 · PDBe 7SI3 · UniProt A0A6I8R0A5

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