Research workbench
Gamma-glutamyl cyclotransferase
Analyse Gamma-glutamyl cyclotransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CRY
- Type
- protein
- Length
- 338 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-glutamyl cyclotransferase
- UniProt
- O75223
- Pockets
- 7 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-glutamyl cyclotransferase | protein | 169 | 31% helix, 38% strand | O75223 |
| B | Gamma-glutamyl cyclotransferase | protein | 169 | 30% helix, 38% strand | O75223 |
Ligands and binding sites
- ACT · Acetate ion · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.65 | 0.83 | 40 | ACT |
| 2 | 211 | 0.63 | 0.83 | 34 | ACT |
| 3 | 147 | 0.59 | 0.83 | 23 | empty |
| 4 | 142 | 0.57 | 0.83 | 26 | empty |
| 5 | 203 | 0.51 | 0.76 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 889 Ų buried · 20 hydrogen bonds · protein-protein
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 O75223
- Elsewhere: RCSB PDB 3CRY · PDBe 3CRY · UniProt O75223
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.