MolNFT v1 · #129304 · protein
Endothiapepsin in complex with hydrazide fragment
5OG7: “Endothiapepsin in complex with hydrazide fragment”. X-ray diffraction, 1 ligand (FLK), 1 pocket (best druggability 0.57). MolNFT v1 #129304 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OG7
- 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
- Ligands
- FLK
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endothiapepsin (EC 3.4.23.22) | protein | 330 | 11% helix, 45% strand | P11838 |
Ligands and binding sites
- FLK · 3-chloranyl-~{N}'-(4,5-dihydro-1~{H}-imidazol-3-ium-2-yl)propanehydrazide · ligand · chains A
- DMS · Dimethyl sulfoxide · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 292 | 0.57 | 0.77 | 39 | DMS, FLK |
Modifications
Observed in the structure: 1 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 P11838
- Elsewhere: RCSB PDB 5OG7 · PDBe 5OG7 · UniProt P11838
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