Research workbench
Pandda analysis group deposition -- auto-refined data of endothiapepsin for ground state model 13, dmso-free
Analyse Pandda analysis group deposition -- auto-refined data of endothiapepsin for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5R2P
- Type
- protein
- Length
- 330 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endothiapepsin
- EC
- 3.4.23.22
- UniProt
- P11838
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endothiapepsin (EC 3.4.23.22) | protein | 330 | 10% helix, 45% strand | P11838 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 320 | 0.57 | 0.76 | 35 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5R2P · PanDDA analysis group deposition -- Auto-refined data of Endothiapepsin for ground state… · the same entry in another collection · chain A against A, TM-score 1.00
- P11838 · AlphaFold monomer V2.0 prediction for endothiapepsin (P11838) · a predicted model of the same protein · 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 P11838
- Elsewhere: RCSB PDB 5R2P · PDBe 5R2P · UniProt P11838
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