Research workbench
Bovine alpha-CHYMOTRYPSIN:BPTI crystallization
Analyse Bovine alpha-CHYMOTRYPSIN:BPTI crystallization in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MTN
- Type
- protein
- Length
- 594 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-chymotrypsin; Basic pancreatic trypsin inhibitor
- EC
- 3.4.21.1
- UniProt
- P00766, P00974
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 4 distinct chains · 13% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Alpha-chymotrypsin (EC 3.4.21.1) | protein | 11 | 0% helix, 0% strand | P00766 |
| B, F | Alpha-chymotrypsin (EC 3.4.21.1) | protein | 131 | 2% helix, 37% strand | P00766 |
| C, G | Alpha-chymotrypsin (EC 3.4.21.1) | protein | 97 | 26% helix, 36% strand | P00766 |
| D, H | Basic pancreatic trypsin inhibitor | protein | 58 | 19% helix, 28% strand | P00974 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains D, H, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 403 | 0.64 | 0.78 | 38 | SO4 |
| 2 | 430 | 0.63 | 0.77 | 39 | SO4 |
| 3 | 159 | 0.59 | 0.83 | 32 | SO4 |
| 4 | 98 | 0.44 | 0.79 | 16 | SO4 |
Interfaces
15 interfaces between chains.
- F–G · 3032 Ų buried · 49 hydrogen bonds · protein-protein
- B–C · 2981 Ų buried · 46 hydrogen bonds · protein-protein
- A–B · 513 Ų buried · 2 hydrogen bonds · protein-protein
- E–F · 504 Ų buried · 2 hydrogen bonds · protein-protein
- F–H · 418 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 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
- Every structure of UniProt P00974
- Elsewhere: RCSB PDB 1MTN · PDBe 1MTN · UniProt P00766 · UniProt P00974
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