Research workbench
Electron density calculations as an extension of protein structure refinement. streptomyces griseus protease at 1.5 ångströms resolution
Analyse Electron density calculations as an extension of protein structure refinement.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2SGA
- Type
- protein
- Length
- 181 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteinase a
- UniProt
- P00776
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proteinase a | protein | 181 | 10% helix, 55% strand | P00776 |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2SGA · Electron density calculations as an extension of protein structure refinement.… · 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 2SGA · PDBe 2SGA · UniProt P00776
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