Research workbench
Crystal structure of hPin1 WW domain (5-23) fused with maltose-binding protein
Analyse Crystal structure of hPin1 WW domain (5-23) fused with maltose-binding protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5B3Y
- Type
- protein
- Length
- 382 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.901
- Source
- Escherichia coli K-12; Homo sapiens
- Molecule
- Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1,Maltose-binding periplasmic protein
- UniProt
- Q13526, P0AEX9
- Ligands
- GLC
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · resolution 1.901 · 1 distinct chain · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1,Maltose-binding periplasmic protein | protein | 382 | 44% helix, 20% strand | Q13526, P0AEX9 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 313 | 0.69 | 0.83 | 33 | GLC |
| 2 | 123 | 0.38 | 0.74 | 20 | empty |
| 3 | 60 | 0.37 | 0.79 | 16 | empty |
Compared structures
- 5B3Y · Crystal structure of HPIN1 ww domain (5-23) fused with maltose-binding protein · the same entry in another collection · chain A against A, TM-score 1.00
- Q13526 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase… · a predicted model of the same protein · chain A against A, TM-score 0.18
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 Q13526
- Every structure of UniProt P0AEX9
- Elsewhere: RCSB PDB 5B3Y · PDBe 5B3Y · UniProt Q13526 · UniProt P0AEX9
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