Research workbench
The three-dimensional structure of bacillus amyloliquefaciens subtilisin at 1.8 ångströms and an analysis of the structural consequences of peroxide inactivation
Analyse The three-dimensional structure of bacillus amyloliquefaciens subtilisin at 1.8… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ST2
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Subtilisin bpn'
- EC
- 3.4.21.14
- UniProt
- P00782
- Ligands
- CA, SO4
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Subtilisin bpn' (EC 3.4.21.14) | protein | 275 | 29% helix, 20% strand | P00782 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 modified (oxidation).
Compared structures
- 1ST2 · The three-dimensional structure of bacillus amyloliquefaciens subtilisin at 1.8 ångströms… · the same entry in another collection · chain A against A, TM-score 1.00
- P00782 · AlphaFold monomer V2.0 prediction for subtilisin bpn' (P00782) · 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 P00782
- Elsewhere: RCSB PDB 1ST2 · PDBe 1ST2 · UniProt P00782
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