Research workbench
Human thrombin complex with hirudin variant
Analyse Human thrombin complex with hirudin variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HXF
- Type
- protein
- Length
- 284 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thrombin; Hirudin variant
- EC
- 3.4.21.5
- UniProt
- P00734, P01050
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 3 distinct chains · 16% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Thrombin (EC 3.4.21.5) | protein | 26 | 35% helix, 0% strand | P00734 |
| H | Thrombin (EC 3.4.21.5) | protein | 248 | 13% helix, 36% strand | P00734 |
| I | Hirudin variant | protein | 10 | 30% helix, 0% strand | P01050 |
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 | 293 | 0.57 | 0.77 | 41 | empty |
Interfaces
2 interfaces between chains.
- L–H · 1089 Ų buried · 22 hydrogen bonds · protein-protein
- H–I · 598 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 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 P00734
- Every structure of UniProt P01050
- Elsewhere: RCSB PDB 1HXF · PDBe 1HXF · UniProt P00734 · UniProt P01050
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