Research workbench
Refined crystal structure of gamma-chymotrypsin at 1.9 ångströms resolution
Analyse Refined crystal structure of gamma-chymotrypsin at 1.9 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GCH
- Type
- protein
- Length
- 236 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-chymotrypsin a
- EC
- 3.4.21.1
- UniProt
- P00766
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 3 distinct chains · 10% 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, 37% strand | P00766 |
| G | Gamma-chymotrypsin a (EC 3.4.21.1) | protein | 95 | 21% helix, 37% strand | P00766 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 71 | 0.48 | 0.84 | 24 | empty |
Interfaces
3 interfaces between chains.
- F–G · 2947 Ų buried · 40 hydrogen bonds · protein-protein
- E–F · 488 Ų buried · 1 hydrogen bond · protein-protein
- E–G · 244 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 2GCH · Refined crystal structure of gamma-chymotrypsin at 1.9 ångströms resolution · 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 0.99
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 2GCH · PDBe 2GCH · UniProt P00766
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