Research workbench
UMP/CMP kinase from slime mold
Analyse UMP/CMP kinase from slime mold in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UKE
- Type
- protein
- Length
- 193 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- URIDYLMONOPHOSPHATE/CYTIDYLMONOPHOSPHATE kinase
- EC
- 2.7.4.14
- UniProt
- P20425
- Ligands
- UP5, MG
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | URIDYLMONOPHOSPHATE/CYTIDYLMONOPHOSPHATE kinase (EC 2.7.4.14) | protein | 193 | 53% helix, 15% strand | P20425 |
Ligands and binding sites
- UP5 · P1-(adenosine-5'-P5-(uridine-5')pentaphosphate · ligand · chains A
- MG · Magnesium ion · metal · 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 319 | 0.75 | 0.87 | 43 | MG, UP5 |
Compared structures
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 P20425
- Elsewhere: RCSB PDB 1UKE · PDBe 1UKE · UniProt P20425
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