MolNFT v1 · #90859 · protein
The structure of human glycinamide ribonucleotide transformylase in complex with 10R-methylthio-ddathf.
4EW3 · Trifunctional purine biosynthetic protein adenosine-3: “The structure of human glycinamide ribonucleotide transformylase in complex with 10R-methylthio-ddathf.”. X-ray diffraction, 3 ligands (DXZ, SO4, PO4), 1 pocket (best…
- PDB
- 4EW3
- Type
- protein
- Length
- 205 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trifunctional purine biosynthetic protein adenosine-3
- EC
- 6.3.4.13, 6.3.3.1, 2.1.2.2
- UniProt
- P22102
- Ligands
- DXZ, SO4, PO4
- Pockets
- 1 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trifunctional purine biosynthetic protein adenosine-3 (EC 6.3.4.13, 6.3.3.1, 2.1.2.2) | protein | 205 | 35% helix, 23% strand | P22102 |
Ligands and binding sites
- DXZ · N-({4-[(1R)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(methylsulfanyl)butyl]phenyl}carbonyl)-L-glutamic acid · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- PO4 · Phosphate ion · ion · 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 | 298 | 0.61 | 0.79 | 33 | DXZ |
Compared structures
- 4EW3 · The structure of human glycinamide ribonucleotide transformylase in complex with… · 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 0.96
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 4EW3 · PDBe 4EW3 · UniProt P22102
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