Research workbench
Crystal structure of the B'-a' domain of thermophilic fungal protein disulfide isomerase (oxidized form)
Analyse Crystal structure of the B'-a' domain of thermophilic fungal protein disulfide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WT2
- Type
- protein
- Length
- 726 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein disulfide-isomerase
- EC
- 5.3.4.1
- UniProt
- P55059
- Pockets
- 8 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Protein disulfide-isomerase (EC 5.3.4.1) | protein | 242 | 36% helix, 20% strand | P55059 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 524 | 0.64 | 0.76 | 51 | empty |
| 2 | 496 | 0.63 | 0.76 | 54 | empty |
| 3 | 499 | 0.62 | 0.75 | 46 | empty |
| 4 | 377 | 0.58 | 0.75 | 44 | empty |
| 5 | 288 | 0.57 | 0.77 | 29 | empty |
Interfaces
3 interfaces between chains.
- B–C · 228 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 179 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 174 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 3WT2 · Crystal structure of the b'-a' domain of thermophilic fungal protein disulfide isomerase… · the same entry in another collection · chain A against A, TM-score 1.00
- P55059 · AlphaFold monomer V2.0 prediction for protein disulfide-isomerase (P55059) · a predicted model of the same protein · chain A against A, TM-score 0.78
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 P55059
- Elsewhere: RCSB PDB 3WT2 · PDBe 3WT2 · UniProt P55059
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