Research workbench
Endothiapepsin complex with H189
Analyse Endothiapepsin complex with H189 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GVU
- Type
- protein
- Length
- 334 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endothiapepsin; Inhibitor, H189
- EC
- 3.4.23.22
- UniProt
- P11838
- Ligands
- SUI, SO4
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endothiapepsin (EC 3.4.23.22) | protein | 328 | 11% helix, 46% strand | P11838 |
| I | Inhibitor, H189 | protein | 6 | 0% helix, 33% strand | — |
Ligands and binding sites
- SUI · (3-amino-2,5-dioxo-1-pyrrolidinyl)acetic acid · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–I · 685 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent, 1 disulfide, 1 modified (covalent ligand, disulfide, 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 P11838
- Elsewhere: RCSB PDB 1GVU · PDBe 1GVU · UniProt P11838
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