MolNFT v1 · #298187 · protein
AlphaFold monomer V2.0 prediction for alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit phnh (P16686)
P16686: “AlphaFold monomer V2.0 prediction for alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit phnh…”. MolNFT v1 #298187 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P16686
- Type
- protein
- Length
- 194 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x40B9C9d5F084D34d026E9d5Dd10501AcdF6d6152
- Molecule
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit phnh
- UniProt
- P16686
Structure
1 distinct chain · 32% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit phnh | protein | 194 | 32% helix, 21% strand | P16686 |
Compared structures
- 4XB6 · Structure of the E. COLI C-P lyase core complex · an experimental structure of the same protein · chain A against B, TM-score 0.99
- 7Z15 · E. coli C-P lyase bound to a PhnK/PhnL dual ABC dimer and ADP + Pi · an experimental structure of the same protein · chain A against B, TM-score 0.99
- 2FSU · Crystal Structure of the PhnH Protein from Escherichia Coli · an experimental structure of the same protein · chain A against A, TM-score 0.86
- 2FSU · Crystal structure of the phnh protein from escherichia COLI · an experimental structure of the same protein · chain A against A, TM-score 0.86
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 P16686
- Elsewhere: UniProt P16686 · AlphaFold DB P16686
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.