Research workbench
Human gar transformylase in complex with gar and N-({5-[(2-amino-4- oxo-4,7-dihydro-3H-PYRROLO[2,3-D]PYRIMIDIN-6-YL)PROPYL]THIOPHEN-2- YL}CARBONYL)-L-glutamic acid (AGF94)
Analyse Human gar transformylase in complex with gar and N-({5-[(2-amino-4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZYW
- Type
- protein
- Length
- 200 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trifunctional purine biosynthetic protein adenosine-3
- EC
- 2.1.2.2
- UniProt
- P22102
- Ligands
- GAR, G94
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trifunctional purine biosynthetic protein adenosine-3 (EC 2.1.2.2) | protein | 200 | 37% helix, 24% strand | P22102 |
Ligands and binding sites
- GAR · Glycinamide ribonucleotide · ligand · chains A
- G94 · N-({5-[3-(2-amino-4-oxo-4,7-dihydro-1H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]thiophen-2-yl}carbonyl)-L-glutamic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 310 | 0.64 | 0.80 | 39 | GAR, G94 |
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 P22102
- Elsewhere: RCSB PDB 4ZYW · PDBe 4ZYW · UniProt P22102
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