Research workbench
Human gamma-glutamyl cyclotransferase
Analyse Human 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
- 2PN7
- Type
- protein
- Length
- 338 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human gamma-glutamyl cyclotransferase
- EC
- 2.3.2.4
- UniProt
- O75223
- Pockets
- 8 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Human gamma-glutamyl cyclotransferase (EC 2.3.2.4) | protein | 169 | 31% helix, 37% strand | O75223 |
| B | Human gamma-glutamyl cyclotransferase (EC 2.3.2.4) | protein | 169 | 28% helix, 37% strand | O75223 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 211 | 0.62 | 0.82 | 35 | empty |
| 2 | 192 | 0.62 | 0.83 | 37 | empty |
| 3 | 147 | 0.57 | 0.82 | 24 | empty |
| 4 | 130 | 0.55 | 0.82 | 22 | empty |
| 5 | 202 | 0.51 | 0.76 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 893 Ų buried · 18 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 2PN7 · PDBe 2PN7 · UniProt O75223
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