MolNFT v1 · #15020 · protein
Studies on crystal structures active center geometry and depurine mechanism of two ribosome-inactivating proteins
1MRK · Alpha-trichosanthin: “Studies on crystal structures active center geometry and depurine mechanism of two ribosome-inactivating…”. X-ray diffraction, 1 ligand (FMC), 2 pockets (best druggability 0.50). MolNFT v1 #15020 on GenesisL1…
- PDB
- 1MRK
- Type
- protein
- Length
- 247 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-trichosanthin
- UniProt
- P09989
- Ligands
- FMC
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-trichosanthin | protein | 247 | 40% helix, 25% strand | P09989 |
Ligands and binding sites
- FMC · (1S)-1-(7-amino-1H-pyrazolo[4,3-d]pyrimidin-3-yl)-1,4-anhydro-D-ribitol · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.50 | 0.79 | 20 | FMC |
| 2 | 75 | 0.34 | 0.75 | 15 | empty |
Compared structures
- 1MRK · Studies on crystal structures active center geometry and depurine mechanism of two… · the same entry in another collection · chain A against A, TM-score 1.00
- P09989 · AlphaFold monomer V2.0 prediction for ribosome-inactivating protein alpha-trichosanthin… · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P09989
- Elsewhere: RCSB PDB 1MRK · PDBe 1MRK · UniProt P09989
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