Research workbench
Crystal structure of the human glutaminyl cyclase mutant D305A at 1.78 ångström resolution
Analyse Crystal structure of the human glutaminyl cyclase mutant D305A at 1.78 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZEN
- Type
- protein
- Length
- 644 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutaminyl-peptide cyclotransferase
- EC
- 2.3.2.5
- UniProt
- Q16769
- Ligands
- ZN, SO4
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) | protein | 323 | 37% helix, 16% strand | Q16769 |
| B | Glutaminyl-peptide cyclotransferase (EC 2.3.2.5) | protein | 321 | 40% helix, 19% strand | Q16769 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 748 | 0.70 | 0.77 | 104 | empty |
| 2 | 90 | 0.51 | 0.83 | 19 | SO4 |
Interfaces
1 interface between chains.
- A–B · 566 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2ZEN · Crystal structure of the human glutaminyl cyclase mutant D305A at 1.78 angstrom resolution · 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 2ZEN · PDBe 2ZEN · UniProt Q16769
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