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Structure of gamma-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that gamma-chymotrypsin is a covalent acyl-enzyme adduct at low pH
Analyse Structure of gamma-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GCT
- Type
- protein
- Length
- 240 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-chymotrypsin a; Tetrapeptide adduct
- EC
- 3.4.21.1
- UniProt
- P00766
- Ligands
- SO4
Structure
x-ray diffraction · 4 distinct chains · 11% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-chymotrypsin a (EC 3.4.21.1) | protein | 10 | 0% helix, 0% strand | P00766 |
| B | Gamma-chymotrypsin a (EC 3.4.21.1) | protein | 131 | 2% helix, 38% strand | P00766 |
| C | Gamma-chymotrypsin a (EC 3.4.21.1) | protein | 95 | 25% helix, 39% strand | P00766 |
| D | Tetrapeptide adduct | protein | 4 | 0% helix, 50% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
5 interfaces between chains.
- B–C · 2871 Ų buried · 40 hydrogen bonds · protein-protein
- A–B · 492 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 350 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 240 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 76 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 2GCT · Structure of gamma-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that… · the same entry in another collection · chain A against A, TM-score 1.00
- P00766 · AlphaFold monomer V2.0 prediction for chymotrypsinogen a (P00766) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 2GCT · PDBe 2GCT · UniProt P00766
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