UniProt P30101
Protein disulfide-isomerase A3 (P30101)
Protein disulfide-isomerase A3 (UniProt P30101), EC 5.3.4.1: 13 experimental structures on GenesisL1, 1 ligand bound, 15 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- P30101
- Protein
- Protein disulfide-isomerase A3
- EC
- 5.3.4.1
- Experimental structures
- 13
- Predicted models
- 0
- Ligands
- 1
- Pockets
- 15 · 2 records with a druggable one
Structures
13 records of P30101 in the MolNFT archive: 13 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 2ALB | NMR structure of the N-terminal domain a of the glycoprotein chaperone ERp57 | solution nmr | A | — | — |
| 2ALB | NMR structure of the N-terminal domain a of the glycoprotein chaperone ERP57 | solution nmr | A | — | — |
| 2DMM | The solution structure of the second thioredoxin domain of human Protein disulfide-isomerase A3 | solution nmr | A | — | — |
| 2DMM | The solution structure of the second thioredoxin domain of human protein disulfide-isomerase A3 | solution nmr | A | — | — |
| 2H8L | Crystal structure of the bb' fragment of ERp57 | x-ray diffraction | A, B, C | — | — |
| 2H8L | Crystal structure of the bb' fragment of ERP57 | x-ray diffraction | A, B, C | — | — |
| 3F8U | Tapasin/ERp57 heterodimer | x-ray diffraction | A, C | — | — |
| 3F8U | TAPASIN/ERP57 heterodimer | x-ray diffraction | A, C | — | — |
| 6ENY | Structure of the human PLC editing module | electron microscopy | D | — | 8 (best 0.84) |
| 6ENY | Structure of the human plc editing module | electron microscopy | D | — | — |
| 7QNG | Structure of a MHC I-Tapasin-ERp57 complex | x-ray diffraction | B | NAG | 7 (best 0.66) |
| 7QPD | Structure of the human MHC I peptide-loading complex editing module | electron microscopy | E | NAG | — |
| P30101 | AlphaFold monomer V2.0 prediction for protein disulfide-isomerase A3 (P30101) | — | — | — |
Ligands
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · in 2 records
Elsewhere
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