Research workbench
Porcine pepsin in complex with amprenavir
Analyse Porcine pepsin in complex with amprenavir in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XCT
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pepsin a
- EC
- 3.4.23.1
- UniProt
- P00791
- Ligands
- 478
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pepsin a (EC 3.4.23.1) | protein | 323 | 16% helix, 45% strand | P00791 |
Ligands and binding sites
- 478 · {3-[(4-amino-benzenesulfonyl)-isobutyl-amino]-1-benzyl-2-hydroxy-propyl}-carbamic acid tetrahydro-furan-3-yl ester · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 299 | 0.65 | 0.81 | 41 | 478 |
| 2 | 61 | 0.30 | 0.75 | 16 | empty |
Modifications
Observed in the structure: 3 disulfide, 1 modified (disulfide, phosphorylation).
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 P00791
- Elsewhere: RCSB PDB 6XCT · PDBe 6XCT · UniProt P00791
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