MolNFT v1 · #28806 · protein
High resolution structure of bovine alpha-chymotrypsin
1YPH · Chymotrypsin a, chain a: “High resolution structure of bovine alpha-chymotrypsin”. X-ray diffraction, 1 ligand (SO4), 4 pockets (best druggability 0.84). MolNFT v1 #28806 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1YPH
- Type
- protein
- Length
- 478 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chymotrypsin a, chain a; Chymotrypsin a, chain B; Chymotrypsin a, chain C
- EC
- 3.4.21.1
- UniProt
- P00766
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 11% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chymotrypsin a, chain a (EC 3.4.21.1) | protein | 10 | 0% helix, 0% strand | P00766 |
| C, D | Chymotrypsin a, chain B (EC 3.4.21.1) | protein | 131 | 2% helix, 38% strand | P00766 |
| E, F | Chymotrypsin a, chain C (EC 3.4.21.1) | protein | 97 | 26% helix, 37% strand | P00766 |
| B | Chymotrypsin a, chain a (EC 3.4.21.1) | protein | 12 | 0% helix, 0% strand | P00766 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains C, E, F, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 469 | 0.84 | 0.91 | 97 | empty |
| 2 | 117 | 0.47 | 0.79 | 26 | SO4 |
| 3 | 109 | 0.41 | 0.76 | 21 | empty |
| 4 | 102 | 0.40 | 0.76 | 20 | SO4 |
Interfaces
10 interfaces between chains.
- D–F · 3027 Ų buried · 43 hydrogen bonds · protein-protein
- C–E · 3006 Ų buried · 51 hydrogen bonds · protein-protein
- B–D · 495 Ų buried · 1 hydrogen bond · protein-protein
- C–D · 478 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 472 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 10 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 1YPH · PDBe 1YPH · UniProt P00766
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