Research workbench
PH influences fluoride coordination number of the alfx phosphoryl transfer transition state analog
Analyse PH influences fluoride coordination number of the alfx phosphoryl transfer… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UKD
- Type
- protein
- Length
- 194 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
- ADP, C5P, AF3, MG
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | URIDYLMONOPHOSPHATE/CYTIDYLMONOPHOSPHATE kinase (EC 2.7.4.14) | protein | 194 | 54% helix, 15% strand | P20425 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- C5P · Cytidine-5'-monophosphate · ligand · chains A
- AF3 · Aluminum fluoride · 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 | 266 | 0.71 | 0.86 | 43 | MG, ADP, C5P, AF3 |
Compared structures
- 5UKD · PH influences fluoride coordination number of the alfx phosphoryl transfer transition… · the same entry in another collection · chain A against A, TM-score 1.00
- P20425 · AlphaFold monomer V2.0 prediction for ump-cmp kinase (P20425) · 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 P20425
- Elsewhere: RCSB PDB 5UKD · PDBe 5UKD · UniProt P20425
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