Research workbench
Gamma-chymotrypsin is a complex of alpha-chymotrypsin with its own autolysis products
Analyse Gamma-chymotrypsin is a complex of alpha-chymotrypsin with its own autolysis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8GCH
- Type
- protein
- Length
- 240 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-chymotrypsin a; Gly ala TRP peptide
- EC
- 3.4.21.1
- UniProt
- P00766
- Ligands
- SO4
Structure
x-ray diffraction · 4 distinct chains · 11% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Gamma-chymotrypsin a (EC 3.4.21.1) | protein | 10 | 0% helix, 0% strand | P00766 |
| F | Gamma-chymotrypsin a (EC 3.4.21.1) | protein | 131 | 2% helix, 38% strand | P00766 |
| G | Gamma-chymotrypsin a (EC 3.4.21.1) | protein | 96 | 25% helix, 38% strand | P00766 |
| C | Gly ala TRP peptide | protein | 3 | 0% helix, 33% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains F, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
5 interfaces between chains.
- F–G · 2998 Ų buried · 45 hydrogen bonds · protein-protein
- E–F · 490 Ų buried · 1 hydrogen bond · protein-protein
- G–C · 295 Ų buried · 11 hydrogen bonds · protein-protein
- E–G · 250 Ų buried · 2 hydrogen bonds · protein-protein
- F–C · 75 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 8GCH · Gamma-chymotrypsin is a complex of alpha-chymotrypsin with its own autolysis products · the same entry in another collection · chain E against E, TM-score 1.00
- P00766 · AlphaFold monomer V2.0 prediction for chymotrypsinogen a (P00766) · a predicted model of the same protein · chain G against A, TM-score 0.98
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 P00766
- Elsewhere: RCSB PDB 8GCH · PDBe 8GCH · UniProt P00766
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