Research workbench
Non-covalent complex between alpha-1-pi-pittsburgh and S195A trypsin
Analyse Non-covalent complex between alpha-1-pi-pittsburgh and S195A trypsin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OPH
- Type
- protein
- Length
- 598 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-1-antitrypsin precursor; Trypsinogen, cationic precursor
- EC
- 3.4.21.4
- UniProt
- P01009, P00760
- Pockets
- 5 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-1-antitrypsin precursor | protein | 375 | 31% helix, 33% strand | P01009 |
| B | Trypsinogen, cationic precursor (EC 3.4.21.4) | protein | 223 | 10% helix, 36% strand | P00760 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 369 | 0.64 | 0.79 | 37 | empty |
| 2 | 122 | 0.55 | 0.82 | 18 | empty |
| 3 | 221 | 0.50 | 0.75 | 33 | empty |
| 4 | 88 | 0.40 | 0.78 | 16 | empty |
| 5 | 55 | 0.34 | 0.78 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 698 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 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 P01009
- Every structure of UniProt P00760
- Elsewhere: RCSB PDB 1OPH · PDBe 1OPH · UniProt P01009 · UniProt P00760
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