Research workbench
The serine protease domain of enteropeptidase bound to inhibitor val- asp-asp-asp-asp-lys-chloromethane
Analyse The serine protease domain of enteropeptidase bound to inhibitor val… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EKB
- Type
- protein
- Length
- 246 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enteropeptidase; Val-asp-asp-asp-asp-lyk peptide
- EC
- 3.4.21.9
- UniProt
- P98072
- Ligands
- ZN, 0QE
Structure
x-ray diffraction · 3 distinct chains · 9% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enteropeptidase (EC 3.4.21.9) | protein | 7 | 0% helix, 0% strand | P98072 |
| B | Enteropeptidase (EC 3.4.21.9) | protein | 235 | 9% helix, 37% strand | P98072 |
| C | Val-asp-asp-asp-asp-lyk peptide | protein | 4 | 0% helix, 25% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
2 interfaces between chains.
- A–B · 453 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 416 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
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 P98072
- Elsewhere: RCSB PDB 1EKB · PDBe 1EKB · UniProt P98072
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