MolNFT v1 · #55395 · protein

Conformational changes in the catalytic domain of the cpx- ATPase copb-B upon nucleotide binding

2YJ3 · Copper-transporting ATPase: “Conformational changes in the catalytic domain of the cpx- ATPase copb-B upon nucleotide binding”. X-ray diffraction, 2 ligands (MG, SO4), 2 pockets (best druggability 0.60). MolNFT v1 #55395 on…

PDB: 2YJ3
Type: protein
Length: 236 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Copper-transporting ATPase
EC: 3.6.1.36, 3.6.3.10
UniProt: Q97UU7
Ligands: MG, SO4
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Copper-transporting ATPase (EC 3.6.1.36, 3.6.3.10)	protein	236	38% helix, 29% strand	Q97UU7

Ligands and binding sites

MG · Magnesium ion · metal · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	129	0.60	0.85	24	empty
2	330	0.59	0.77	40	SO4, GOL

Compared structures

2YJ3 · Conformational changes in the catalytic domain of the CPx-ATPase CopB- B upon nucleotide… · 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 Q97UU7
Elsewhere: RCSB PDB 2YJ3 · PDBe 2YJ3 · UniProt Q97UU7

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