MolNFT v1 · #24117 · protein
Substrate specificity and assembly of catalytic center derived from two structures of ligated uridylate kinase
1UKZ: “Substrate specificity and assembly of catalytic center derived from two structures of ligated uridylate kinase”. X-ray diffraction, 2 ligands (ADP, AMP), 1 pocket (best druggability 0.75). MolNFT v1 #24117 on GenesisL1: 3D…
- PDB
- 1UKZ
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uridylate kinase
- EC
- 2.7.4.-
- UniProt
- P15700
- Ligands
- ADP, AMP
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uridylate kinase (EC 2.7.4.-) | protein | 196 | 57% helix, 13% strand | P15700 |
Ligands and binding sites
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 290 | 0.75 | 0.88 | 45 | ADP, AMP |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1UKZ · Substrate specificity and assembly of catalytic center derived from two structures of… · the same entry in another collection · chain A against A, TM-score 1.00
- P15700 · AlphaFold monomer V2.0 prediction for uridylate kinase (P15700) · 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 P15700
- Elsewhere: RCSB PDB 1UKZ · PDBe 1UKZ · UniProt P15700
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.