Research workbench
Inward facing conformation of MHP1
Analyse Inward facing conformation of MHP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X79
- Type
- protein
- Length
- 465 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydantoin transport protein
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydantoin transport protein | protein | 465 | 63% helix, 0% strand | — |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 981 | 0.79 | 0.81 | 90 | empty |
| 2 | 91 | 0.37 | 0.76 | 16 | empty |
| 3 | 84 | 0.36 | 0.76 | 14 | empty |
| 4 | 60 | 0.36 | 0.78 | 16 | empty |
Modifications
Observed in the structure: 19 modified (engineered).
Compared structures
- 2X79 · Inward facing conformation of Mhp1 · 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
- Elsewhere: RCSB PDB 2X79 · PDBe 2X79
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