Research workbench
Alternative conformations of the X region of human protein disulphide- isomerase modulate exposure of the substrate binding B' domain
Analyse Alternative conformations of the X region of human protein disulphide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BJ5
- Type
- protein
- Length
- 130 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein disulfide-isomerase
- EC
- 5.3.4.1
- UniProt
- P07237
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein disulfide-isomerase (EC 5.3.4.1) | protein | 130 | 35% helix, 20% strand | P07237 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3BJ5 · Alternative conformations of the x region of human protein disulphide-isomerase modulate… · the same entry in another collection · chain A against A, TM-score 1.00
- P07237 · AlphaFold monomer V2.0 prediction for protein disulfide-isomerase (P07237) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 P07237
- Elsewhere: RCSB PDB 3BJ5 · PDBe 3BJ5 · UniProt P07237
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