Research workbench
Crystal structure of bovine alpha-chymotrypsin in space group P65
Analyse Crystal structure of bovine alpha-chymotrypsin in space group P65 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DI8
- Type
- protein
- Length
- 964 residues
- Chains
- 12
- 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
- 11 · best druggability 0.87
Structure
x-ray diffraction · 3 distinct chains · 11% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, G, J | Chymotrypsin a chain a (EC 3.4.21.1) | protein | 13 | 0% helix, 0% strand | P00766 |
| B, E, H, K | Chymotrypsin a chain B (EC 3.4.21.1) | protein | 131 | 2% helix, 39% strand | P00766 |
| C, F, I, L | Chymotrypsin a chain C (EC 3.4.21.1) | protein | 97 | 25% helix, 38% strand | P00766 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 13 copies · chains B, C, E, F, H, I, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1089 | 0.87 | 0.88 | 146 | empty |
| 2 | 398 | 0.64 | 0.78 | 50 | empty |
| 3 | 407 | 0.63 | 0.77 | 51 | empty |
| 4 | 134 | 0.60 | 0.85 | 36 | empty |
| 5 | 214 | 0.58 | 0.80 | 44 | empty |
Interfaces
50 interfaces between chains.
- H–I · 3009 Ų buried · 45 hydrogen bonds · protein-protein
- E–F · 3004 Ų buried · 43 hydrogen bonds · protein-protein
- K–L · 2994 Ų buried · 45 hydrogen bonds · protein-protein
- B–C · 2973 Ų buried · 47 hydrogen bonds · protein-protein
- G–H · 546 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 disulfide (disulfide).
Compared structures
- 6DI8 · Crystal structure of bovine alpha-chymotrypsin in space group P65 · the same entry in another collection · chain L against L, TM-score 1.00
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 6DI8 · PDBe 6DI8 · UniProt P00766
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