MolNFT v1 · #136825 · protein
Crystal structure of mppr-1I
5V50 · Pr-1 protein: “Crystal structure of mppr-1I”. X-ray diffraction, 5 pockets (best druggability 0.59). MolNFT v1 #136825 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5V50
- Type
- protein
- Length
- 936 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pr-1 protein
- UniProt
- H6U756
- Pockets
- 5 · best druggability 0.59
Structure
x-ray diffraction · 5 distinct chains · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Pr-1 protein | protein | 134 | 44% helix, 19% strand | H6U756 |
| B, D | Pr-1 protein | protein | 133 | 39% helix, 19% strand | H6U756 |
| C | Pr-1 protein | protein | 129 | 40% helix, 19% strand | H6U756 |
| F | Pr-1 protein | protein | 138 | 38% helix, 20% strand | H6U756 |
| G | Pr-1 protein | protein | 135 | 41% helix, 20% strand | H6U756 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.59 | 0.91 | 18 | empty |
| 2 | 57 | 0.43 | 0.82 | 19 | empty |
| 3 | 54 | 0.33 | 0.77 | 14 | empty |
| 4 | 55 | 0.32 | 0.76 | 13 | empty |
| 5 | 50 | 0.29 | 0.75 | 12 | empty |
Interfaces
6 interfaces between chains.
- E–F · 861 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 853 Ų buried · 10 hydrogen bonds · protein-protein
- D–E · 849 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 821 Ų buried · 9 hydrogen bonds · protein-protein
- F–G · 809 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide (disulfide).
Compared structures
- 5V50 · Crystal Structure of MpPR-1i · the same entry in another collection · 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 H6U756
- Elsewhere: RCSB PDB 5V50 · PDBe 5V50 · UniProt H6U756
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