MolNFT v1 · #24058 · protein
Crystal structure of human uridine-cytidine kinase 2 complexed with products, cmp and ADP
1UJ2: “Crystal structure of human uridine-cytidine kinase 2 complexed with products, cmp and ADP”. X-ray diffraction, 3 ligands (C5P, ADP, MG), 2 pockets (best druggability 0.65). MolNFT v1 #24058 on GenesisL1: 3D structure, binding sites…
- PDB
- 1UJ2
- Type
- protein
- Length
- 426 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uridine-cytidine kinase 2
- EC
- 2.7.1.48
- UniProt
- Q9BZX2
- Ligands
- C5P, ADP, MG
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Uridine-cytidine kinase 2 (EC 2.7.1.48) | protein | 213 | 52% helix, 21% strand | Q9BZX2 |
Ligands and binding sites
- C5P · Cytidine-5'-monophosphate · ligand · 2 copies · chains A, B
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 342 | 0.65 | 0.80 | 45 | MG, C5P, ADP |
| 2 | 320 | 0.62 | 0.79 | 45 | MG, C5P, ADP |
Interfaces
1 interface between chains.
- A–B · 784 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 1UJ2 · Crystal structure of human uridine-cytidine kinase 2 complexed with products, CMP and ADP · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BZX2 · AlphaFold monomer V2.0 prediction for uridine-cytidine kinase 2 (Q9BZX2) · a predicted model of the same protein · chain A 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 Q9BZX2
- Elsewhere: RCSB PDB 1UJ2 · PDBe 1UJ2 · UniProt Q9BZX2
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