Research workbench
Extracellular domain of human hepsin
Analyse Extracellular domain of human hepsin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P57
- Type
- protein
- Length
- 357 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine protease hepsin
- EC
- 3.4.21.-
- UniProt
- P05981
- Ligands
- CR4
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine protease hepsin (EC 3.4.21.-) | protein | 110 | 20% helix, 35% strand | P05981 |
| B | Serine protease hepsin (EC 3.4.21.-) | protein | 247 | 11% helix, 37% strand | P05981 |
Ligands and binding sites
- CR4 · 2-{5-[amino(iminio)methyl]-1H-benzimidazol-2-yl}benzenolate · ligand · chains B
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 | 94 | 0.42 | 0.78 | 28 | CR4 |
| 2 | 87 | 0.41 | 0.78 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1248 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
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 P05981
- Elsewhere: RCSB PDB 1P57 · PDBe 1P57 · UniProt P05981
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