Research workbench
The structure of human glycinamide ribonucleotide transformylase in complex with ALPHA,BETA-N-(hydroxyacetyl)-D-ribofuranosylamine and 10-formyl-5,8,DIDEAZAFOLATE
Analyse The structure of human glycinamide ribonucleotide transformylase in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZLY
- Type
- protein
- Length
- 200 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoribosylglycinamide formyltransferase
- EC
- 2.1.2.2
- UniProt
- P22102
- Ligands
- GRF, DQB
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) | protein | 200 | 34% helix, 23% strand | P22102 |
Ligands and binding sites
- GRF · 5-O-phosphono-beta-D-ribofuranosylamine · ligand · chains A
- DQB · 4-[(4-{[(2-amino-4-oxo-3,4-dihydroquinazolin-6-yl)methyl]amino}benzoyl)amino]butanoic 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 | 382 | 0.62 | 0.77 | 37 | GRF, DQB |
Compared structures
- 1ZLY · 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 0.99
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 1ZLY · PDBe 1ZLY · UniProt P22102
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