Research workbench
Crystal structure of the catalytic domain of human golgi-resident glutaminyl cyclase in complex with N-acetylhistamine
Analyse Crystal structure of the catalytic domain of human golgi-resident glutaminyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PB8
- Type
- protein
- Length
- 313 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutaminyl-peptide cyclotransferase-like protein
- EC
- 2.3.2.5
- UniProt
- Q9NXS2
- Ligands
- AHN, ZN
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Glutaminyl-peptide cyclotransferase-like protein (EC 2.3.2.5) | protein | 313 | 40% helix, 18% strand | Q9NXS2 |
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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.43 | 0.77 | 22 | AHN, ZN |
| 2 | 54 | 0.38 | 0.80 | 13 | empty |
Compared structures
- 3PB8 · Crystal structure of the catalytic domain of human Golgi-resident glutaminyl cyclase in… · the same entry in another collection · chain X against X, TM-score 1.00
- Q9NXS2 · AlphaFold monomer V2.0 prediction for glutaminyl-peptide cyclotransferase-like protein… · a predicted model of the same protein · chain X against A, TM-score 0.99
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 Q9NXS2
- Elsewhere: RCSB PDB 3PB8 · PDBe 3PB8 · UniProt Q9NXS2
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