Research workbench
Structure of human GGT1 in complex with abba
Analyse Structure of human GGT1 in complex with abba in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LD9
- Type
- protein
- Length
- 532 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione hydrolase 1 heavy chain; Glutathione hydrolase 1 light chain
- EC
- 3.4.19.13, 2.3.2.2, 3.4.19.14
- UniProt
- P19440
- Ligands
- XUJ, XU7, NAG, NA, CL
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione hydrolase 1 heavy chain (EC 3.4.19.13, 2.3.2.2, 3.4.19.14) | protein | 343 | 51% helix, 13% strand | P19440 |
| B | Glutathione hydrolase 1 light chain (EC 3.4.19.13, 2.3.2.2, 3.4.19.14) | protein | 189 | 19% helix, 28% strand | P19440 |
Ligands and binding sites
- XUJ · (2R)-2-amino-4-boronobutanoic acid · ligand · chains A, B
- XU7 · (2S)-2-amino-4-boronobutanoic acid · ligand · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A, B
- NA · Sodium ion · metal · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 600 | 0.74 | 0.82 | 59 | XUJ, XU7, EPE |
| 2 | 72 | 0.38 | 0.78 | 21 | empty |
| 3 | 81 | 0.35 | 0.76 | 19 | empty |
| 4 | 64 | 0.33 | 0.76 | 16 | empty |
| 5 | 56 | 0.32 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 6264 Ų buried · 103 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 glycan, 2 covalent, 1 disulfide (N-glycosylation, covalent ligand, disulfide).
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 P19440
- Elsewhere: RCSB PDB 7LD9 · PDBe 7LD9 · UniProt P19440
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.