Research workbench
Structure of the hirugen and hirulog 1 complexes of alpha-thrombin
Analyse Structure of the hirugen and hirulog 1 complexes of alpha-thrombin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HGT
- Type
- protein
- Length
- 294 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00734, P28504
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | — | protein | 33 | — | P00734 |
| H | — | protein | 253 | — | P00734 |
| I | — | protein | 3 | — | — |
| J | — | protein | 5 | — | P28504 |
Compared structures
- 2HGT · Structure of the hirugen and hirulog 1 complexes of alpha-thrombin · the same entry in another collection · chain L against L, TM-score 1.00
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 P28504
- Elsewhere: RCSB PDB 2HGT · PDBe 2HGT · UniProt P00734 · UniProt P28504
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