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Three-dimensional structure in solution of cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy
Analyse Three-dimensional structure in solution of cucurbita maxima trypsin inhibitor-V… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TIN
- Type
- protein
- Length
- 68 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypsin inhibitor V
- UniProt
- P19873
- Ligands
- ACE
Structure
solution nmr · 1 distinct chain · 16% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypsin inhibitor V | protein | 68 | 16% helix, 24% strand | P19873 |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).
Compared structures
- 1TIN · Three-dimensional structure in solution of cucurbita maxima trypsin inhibitor-V… · the same entry in another collection · chain A against A, TM-score 1.00
- P19873 · AlphaFold monomer V2.0 prediction for inhibitor of trypsin and hageman factor (P19873) · a predicted model of the same protein · chain A against A, TM-score 0.71
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 P19873
- Elsewhere: RCSB PDB 1TIN · PDBe 1TIN · UniProt P19873
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