MolNFT v1 · #169863 · protein
Structure of human GGT1 in complex with full gsh molecule
6XPC: “Structure of human GGT1 in complex with full gsh molecule”. X-ray diffraction, 4 ligands (GSH, NAG, NA). MolNFT v1 #169863 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6XPC
- Type
- protein
- Length
- 531 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P19440
- Ligands
- GSH, NAG, NA, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 342 | — | P19440 |
| B | — | protein | 189 | — | P19440 |
Ligands and binding sites
- GSH · Glutathione · 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
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6XPC · Structure of human GGT1 in complex with full GSH molecule · the same entry in another collection · chain A against A, TM-score 1.00
- P19440 · AlphaFold monomer V2.0 prediction for glutathione hydrolase 1 proenzyme (P19440) · a predicted model of the same protein · chain A 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 P19440
- Elsewhere: RCSB PDB 6XPC · PDBe 6XPC · UniProt P19440
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