MolNFT v1 · #136161 · protein
PH influences fluoride coordination number of the alfx phosphoryl transfer transition state analog
5UKD: “PH influences fluoride coordination number of the alfx phosphoryl transfer transition state analog”. X-ray diffraction, 4 ligands (ADP, C5P, AF3). MolNFT v1 #136161 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5UKD
- Type
- protein
- Length
- 194 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P20425
- Ligands
- ADP, C5P, AF3, MG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 194 | — | 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
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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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