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The 1.8 ångströms structure of the complex between chymostatin and streptomyces griseus protease a. a model for serine protease catalytic tetrahedral intermediates
Analyse The 1.8 ångströms structure of the complex between chymostatin and streptomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SGC
- Type
- protein
- Length
- 185 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteinase a; Chymostatin a
- UniProt
- P00776
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proteinase a | protein | 181 | 10% helix, 55% strand | P00776 |
| B | Chymostatin a | protein | 4 | 0% helix, 25% strand | — |
Interfaces
1 interface between chains.
- A–B · 445 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide, 2 modified (disulfide, nonstandard).
Compared structures
- 1SGC · The 1.8 ångströms structure of the complex between chymostatin and streptomyces griseus… · the same entry in another collection · chain A against A, TM-score 1.00
- P00776 · AlphaFold monomer V2.0 prediction for streptogrisin-a (P00776) · a predicted model of the same protein · 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 P00776
- Elsewhere: RCSB PDB 1SGC · PDBe 1SGC · UniProt P00776
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