Research workbench
Crystal structure of bovine trypsinogen at 1.8 ångströms resolution. II. crystallographic refinement, refined crystal structure and comparison with bovine trypsin
Analyse Crystal structure of bovine trypsinogen at 1.8 ångströms resolution. II.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TGB
- Type
- protein
- Length
- 223 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypsinogen
- UniProt
- P00760
- Ligands
- CA
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypsinogen | protein | 223 | 10% helix, 35% strand | P00760 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 50 | 0.37 | 0.80 | 18 | empty |
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 1TGB · Crystal structure of bovine trypsinogen at 1.8 ångströms resolution. II. crystallographic… · the same entry in another collection · chain A against A, 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 P00760
- Elsewhere: RCSB PDB 1TGB · PDBe 1TGB · UniProt P00760
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