Research workbench
Context dependence of protein secondary structure formation. the three-dimensional structure and stability of a hybrid between chymotrypsin inhibitor 2 and helix E from subtilisin carlsberg
Analyse Context dependence of protein secondary structure formation. the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CIS
- Type
- protein
- Length
- 66 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hybrid protein formed from chymotrypsin inhibitor-2
- UniProt
- P01053
Structure
solution nmr · 1 distinct chain · 17% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hybrid protein formed from chymotrypsin inhibitor-2 | protein | 66 | 17% helix, 24% strand | P01053 |
Compared structures
- 1CIS · Context dependence of protein secondary structure formation. the three-dimensional… · the same entry in another collection · chain A against A, TM-score 1.00
- P01053 · AlphaFold monomer V2.0 prediction for subtilisin-chymotrypsin inhibitor-2A (P01053) · a predicted model of the same protein · chain A against A, TM-score 0.80
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 P01053
- Elsewhere: RCSB PDB 1CIS · PDBe 1CIS · UniProt P01053
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