Research workbench
Proposed amino acid sequence and the 1.63 ångström X-ray crystal structure of a plant cysteine protease ervatamin B: insight into the structural basis of its stability and substrate specificity.
Analyse Proposed amino acid sequence and the 1.63 ångström X-ray crystal structure of a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IWD
- Type
- protein
- Length
- 215 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ervatamin B
- UniProt
- P60994
- Ligands
- THJ
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ervatamin B | protein | 215 | 27% helix, 23% strand | P60994 |
Ligands and binding sites
- THJ · Thiosulfate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide, 1 covalent (disulfide, covalent ligand).
Compared structures
- 1IWD · Proposed Amino Acid Sequence and the 1.63 Angstrom X-ray Crystal Structure of a Plant… · the same entry in another collection · chain A against A, TM-score 1.00
- P60994 · AlphaFold monomer V2.0 prediction for ervatamin-B (P60994) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P60994
- Elsewhere: RCSB PDB 1IWD · PDBe 1IWD · UniProt P60994
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