Research workbench
Crystal structure of human glutaminyl cyclase in complex with glutamine t-butyl ester
Analyse Crystal structure of human glutaminyl cyclase in complex with glutamine t-butyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AFU
- Type
- protein
- Length
- 642 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.22
- Source
- Homo sapiens
- Molecule
- Glutaminyl-peptide cyclotransferase
- EC
- 2.3.2.5
- UniProt
- Q16769
- Ligands
- BGT, ZN
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · resolution 2.22 · 1 distinct chain · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) | protein | 321 | 38% helix, 18% strand | Q16769 |
Ligands and binding sites
- BGT · Tert-butyl D-alpha-glutaminate · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 667 | 0.69 | 0.77 | 100 | empty |
| 2 | 110 | 0.55 | 0.84 | 20 | BGT |
| 3 | 50 | 0.28 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 568 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2AFU · Crystal structure of human glutaminyl cyclase in complex with glutamine T-butyl ester · the same entry in another collection · chain A against A, TM-score 1.00
- Q16769 · AlphaFold monomer V2.0 prediction for glutaminyl-peptide cyclotransferase (Q16769) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q16769
- Elsewhere: RCSB PDB 2AFU · PDBe 2AFU · UniProt Q16769
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