Research workbench
Crystal structure of a SERPIN:PROTEASE complex
Analyse Crystal structure of a SERPIN:PROTEASE complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EZX
- Type
- protein
- Length
- 511 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-1-antitrypsin; Trypsin
- EC
- 3.4.21.4
- UniProt
- P01009, P00760
- Pockets
- 3 · best druggability 0.39
Structure
x-ray diffraction · 3 distinct chains · 24% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-1-antitrypsin | protein | 335 | 32% helix, 35% strand | P01009 |
| B | Alpha-1-antitrypsin | protein | 36 | 0% helix, 47% strand | P01009 |
| C | Trypsin (EC 3.4.21.4) | protein | 140 | 12% helix, 26% strand | P00760 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.39 | 0.82 | 16 | empty |
| 2 | 135 | 0.38 | 0.73 | 26 | empty |
| 3 | 90 | 0.34 | 0.74 | 19 | empty |
Interfaces
2 interfaces between chains.
- A–B · 2477 Ų buried · 33 hydrogen bonds · protein-protein
- A–C · 448 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 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 1EZX · PDBe 1EZX · UniProt P01009 · UniProt P00760
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