MolNFT v1 · #42573 · protein

Solution structure of the nucleotide binding domain of the human menkes protein in the ATP-bound form

2KMX · Copper-transporting ATPase 1: “Solution structure of the nucleotide binding domain of the human menkes protein in the ATP-bound form”. Solution nmr, 1 ligand (ATP), 3 pockets (best druggability 0.54). MolNFT v1 #42573 on GenesisL1…

PDB: 2KMX
Type: protein
Length: 185 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Copper-transporting ATPase 1
EC: 3.6.3.4
UniProt: Q04656
Ligands: ATP
Pockets: 3 · best druggability 0.54

Structure

solution nmr · 1 distinct chain · 28% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Copper-transporting ATPase 1 (EC 3.6.3.4)	protein	185	28% helix, 24% strand	Q04656

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	112	0.54	0.82	21	ATP
2	105	0.40	0.76	16	empty
3	101	0.37	0.75	17	empty

Compared structures

2KMX · Solution structure of the nucleotide binding domain of the human Menkes protein in the… · the same entry in another collection · chain A against A, TM-score 1.00
Q04656 · AlphaFold monomer V2.0 prediction for copper-transporting ATPase 1 (Q04656) · a predicted model of the same protein · chain A against A, TM-score 0.66

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 Q04656
Elsewhere: RCSB PDB 2KMX · PDBe 2KMX · UniProt Q04656

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.