Research workbench
Crystal structure of the catalytic domain of human golgi-resident glutaminyl cyclase in complex with 1-benzylimidazole
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
- 3PB9
- Type
- protein
- Length
- 309 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
- 1BN, ZN
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Glutaminyl-peptide cyclotransferase-like protein (EC 2.3.2.5) | protein | 309 | 40% helix, 17% 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.52 | 0.86 | 19 | empty |
| 2 | 64 | 0.39 | 0.80 | 16 | 1BN |
Compared structures
- 3PB9 · 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 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 Q9NXS2
- Elsewhere: RCSB PDB 3PB9 · PDBe 3PB9 · UniProt Q9NXS2
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