Research workbench

Structure of human dck complexed with 2'-deoxycytidine and ADP, P 43 21 2 space group

Analyse Structure of human dck complexed with 2'-deoxycytidine and ADP, P 43 21 2 space… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1P61
Type: protein
Length: 229 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Deoxycytidine kinase
EC: 2.7.1.74
UniProt: P27707
Ligands: ADP, DCZ
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Deoxycytidine kinase (EC 2.7.1.74)	protein	229	56% helix, 11% strand	P27707

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains B
DCZ · 2'-deoxycytidine · ligand · chains B

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

Pockets

2 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	200	0.65	0.84	34	ADP, DCZ
2	55	0.30	0.75	14	empty

Compared structures

1P61 · Structure of human dCK complexed with 2'-Deoxycytidine and ADP, P 43 21 2 space group · the same entry in another collection · chain B against B, TM-score 1.00
P27707 · AlphaFold monomer V2.0 prediction for deoxycytidine kinase (P27707) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P27707
Elsewhere: RCSB PDB 1P61 · PDBe 1P61 · UniProt P27707

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