Research workbench
Substrate specificity and assembly of catalytic center derived from two structures of ligated uridylate kinase
Analyse Substrate specificity and assembly of catalytic center derived from two… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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
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