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A structural comparison of 21 inhibitor complexes of the aspartic proteinase from endothia parasitica
Analyse A structural comparison of 21 inhibitor complexes of the aspartic proteinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EPL
- Type
- protein
- Length
- 336 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endothiapepsin; PS1, pro-leu-glu-psa-arg-leu
- EC
- 3.4.23.22
- UniProt
- P11838
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Endothiapepsin (EC 3.4.23.22) | protein | 330 | 9% helix, 47% strand | P11838 |
| I | PS1, pro-leu-glu-psa-arg-leu | protein | 6 | 0% helix, 17% strand | — |
Interfaces
1 interface between chains.
- E–I · 748 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, nonstandard).
Compared structures
- 1EPL · A structural comparison of 21 inhibitor complexes of the aspartic proteinase from… · the same entry in another collection · chain E against E, TM-score 1.00
- P11838 · AlphaFold monomer V2.0 prediction for endothiapepsin (P11838) · a predicted model of the same protein · chain E 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 P11838
- Elsewhere: RCSB PDB 1EPL · PDBe 1EPL · UniProt P11838
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