Research workbench
NMR structure of the N-terminal domain a of the glycoprotein chaperone ERP57
Analyse NMR structure of the N-terminal domain a of the glycoprotein chaperone ERP57 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ALB
- Type
- protein
- Length
- 113 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein disulfide-isomerase A3
- EC
- 5.3.4.1
- UniProt
- P30101
Structure
solution nmr · 1 distinct chain · 35% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein disulfide-isomerase A3 (EC 5.3.4.1) | protein | 113 | 35% helix, 19% strand | P30101 |
Compared structures
- 2ALB · NMR structure of the N-terminal domain a of the glycoprotein chaperone ERp57 · the same entry in another collection · chain A against A, TM-score 1.00
- P30101 · AlphaFold monomer V2.0 prediction for protein disulfide-isomerase A3 (P30101) · a predicted model of the same protein · chain A against A, TM-score 0.90
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 P30101
- Elsewhere: RCSB PDB 2ALB · PDBe 2ALB · UniProt P30101
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