MolNFT v1 · #135290 · protein
Potent competitive inhibition of human ribonucleotide reductase by a novel non-nucleoside small molecule
5TUS: “Potent competitive inhibition of human ribonucleotide reductase by a novel non-nucleoside small molecule”. X-ray diffraction, 3 ligands (TTP, 7LL, MG). MolNFT v1 #135290 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5TUS
- Type
- protein
- Length
- 1,451 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P23921
- Ligands
- TTP, 7LL, MG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 720 | — | P23921 |
| B | — | protein | 731 | — | P23921 |
Ligands and binding sites
- TTP · Thymidine-5'-triphosphate · ligand · 2 copies · chains A, B
- 7LL · 2-hydroxy-N'-[(Z)-(2-hydroxynaphthalen-1-yl) methylidene]benzohydrazide · ligand · chains B
- MG · Magnesium ion · metal · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5TUS · Potent competitive inhibition of human ribonucleotide reductase by a novel non-nucleoside… · the same entry in another collection · chain A against A, TM-score 1.00
- P23921 · AlphaFold monomer V2.0 prediction for ribonucleoside-diphosphate reductase large subunit… · a predicted model of the same protein · chain B 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 P23921
- Elsewhere: RCSB PDB 5TUS · PDBe 5TUS · UniProt P23921
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