MolNFT v1 · #14604 · protein
Complex structure of human gar tfase and substrate beta-gar
1MEN · Phosphoribosylglycinamide formyltransferase: “Complex structure of human gar tfase and substrate beta-gar”. X-ray diffraction, 1 ligand (GAR), 5 pockets (best druggability 0.79). MolNFT v1 #14604 on GenesisL1: 3D structure, binding…
- PDB
- 1MEN
- Type
- protein
- Length
- 603 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoribosylglycinamide formyltransferase
- EC
- 2.1.2.2
- UniProt
- P22102
- Ligands
- GAR
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) | protein | 201 | 36% helix, 24% strand | P22102 |
Ligands and binding sites
- GAR · Glycinamide ribonucleotide · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1135 | 0.79 | 0.80 | 102 | GAR |
| 2 | 406 | 0.66 | 0.79 | 46 | GAR |
| 3 | 303 | 0.60 | 0.78 | 36 | empty |
| 4 | 55 | 0.49 | 0.86 | 17 | empty |
| 5 | 210 | 0.47 | 0.74 | 25 | empty |
Interfaces
3 interfaces between chains.
- A–C · 747 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 278 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 93 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1MEN · complex structure of human GAR Tfase and substrate beta-GAR · 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 0.98
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 1MEN · PDBe 1MEN · UniProt P22102
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