Research workbench
Cys-Gly dipeptidase GliJ in complex with Fe3+
Analyse Cys-Gly dipeptidase GliJ in complex with Fe3+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NRY
- Type
- protein
- Length
- 381 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.85
- Source
- Aspergillus fumigatus Af293
- Molecule
- Dipeptidase gliJ
- EC
- 3.4.13.19
- UniProt
- Q4WMJ8
- Ligands
- FE, CL
- Pockets
- 3 · best druggability 0.34
Structure
x-ray diffraction · resolution 1.85 · 1 distinct chain · 51% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dipeptidase gliJ (EC 3.4.13.19) | protein | 381 | 51% helix, 12% strand | Q4WMJ8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.34 | 0.76 | 17 | empty |
| 2 | 59 | 0.34 | 0.77 | 14 | empty |
| 3 | 71 | 0.30 | 0.74 | 19 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
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 Q4WMJ8
- Elsewhere: RCSB PDB 5NRY · PDBe 5NRY · UniProt Q4WMJ8
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