Research workbench
Crystal structure of bovine gamma-chymotrypsin
Analyse Crystal structure of bovine gamma-chymotrypsin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AB9
- Type
- protein
- Length
- 242 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-chymotrypsin; Pentapeptide (tpgvy)
- EC
- 3.4.21.1
- UniProt
- P00766
- Ligands
- SO4
Structure
x-ray diffraction · 4 distinct chains · 11% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-chymotrypsin (EC 3.4.21.1) | protein | 10 | 0% helix, 0% strand | P00766 |
| B | Gamma-chymotrypsin (EC 3.4.21.1) | protein | 131 | 2% helix, 40% strand | P00766 |
| C | Gamma-chymotrypsin (EC 3.4.21.1) | protein | 96 | 25% helix, 40% strand | P00766 |
| D | Pentapeptide (tpgvy) | protein | 5 | 0% helix, 60% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 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 · 2950 Ų buried · 41 hydrogen bonds · protein-protein
- A–B · 469 Ų buried · 1 hydrogen bond · protein-protein
- C–D · 387 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 215 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 69 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 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 P00766
- Elsewhere: RCSB PDB 1AB9 · PDBe 1AB9 · UniProt P00766
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