Research workbench
Dipeptidase (PH0974) from pyrococcus horikoshii OT3
Analyse Dipeptidase (PH0974) from pyrococcus horikoshii OT3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HOW
- Type
- protein
- Length
- 712 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 356AA long hypothetical dipeptidase
- EC
- 3.4.-.-
- UniProt
- O58691
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 356AA long hypothetical dipeptidase (EC 3.4.-.-) | protein | 356 | 35% helix, 26% strand | O58691 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 722 | 0.79 | 0.84 | 68 | empty |
| 2 | 578 | 0.70 | 0.79 | 45 | empty |
| 3 | 109 | 0.51 | 0.82 | 19 | empty |
| 4 | 54 | 0.37 | 0.80 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1274 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 2HOW · Dipeptidase (PH0974) from Pyrococcus horikoshii OT3 · 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 O58691
- Elsewhere: RCSB PDB 2HOW · PDBe 2HOW · UniProt O58691
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