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Dephospho-CoA kinase in complex with ATP

Analyse Dephospho-CoA kinase in complex with ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JJV
Type: protein
Length: 194 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dephospho-CoA kinase
EC: 2.7.1.24
UniProt: P44920
Ligands: ATP, HG, SO4
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dephospho-CoA kinase (EC 2.7.1.24)	protein	194	58% helix, 12% strand	P44920

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
HG · Mercury (II) ion · metal · chains A
SO4 · Sulfate ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	404	0.61	0.76	32	empty

Compared structures

1JJV · Dephospho-CoA kinase in complex with ATP · the same entry in another collection · chain A against A, TM-score 1.00
P44920 · AlphaFold monomer V2.0 prediction for dephospho-CoA kinase (P44920) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P44920
Elsewhere: RCSB PDB 1JJV · PDBe 1JJV · UniProt P44920

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