Research workbench
Human gar transformylase in complex with gar substrate and AGF102 inhibitor
Analyse Human gar transformylase in complex with gar substrate and AGF102 inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JG0
- Type
- protein
- Length
- 200 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P22102
- Ligands
- GAR, V97
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 200 | — | P22102 |
Ligands and binding sites
- GAR · Glycinamide ribonucleotide · ligand · chains A
- V97 · N-{5-[4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl]thiophene-2-carbonyl}-L-glutamic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7JG0 · Human GAR transformylase in complex with GAR substrate and AGF102 inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- P22102 · AlphaFold monomer V2.0 prediction for trifunctional purine biosynthetic protein… · 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 P22102
- Elsewhere: RCSB PDB 7JG0 · PDBe 7JG0 · UniProt P22102
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