Research workbench
Aicar TRANSFORMYLASE/IMP cyclohydrolase (atic) is essential for de novo purine biosynthesis and infection by cryptococcus neoformans
Analyse Aicar TRANSFORMYLASE/IMP cyclohydrolase (atic) is essential for de novo purine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MGQ
- Type
- protein
- Length
- 2,392 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
- EC
- 2.1.2.3, 3.5.4.10
- UniProt
- A0A225ZZG7
- Ligands
- MG
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase (EC 2.1.2.3, 3.5.4.10) | protein | 602 | 43% helix, 17% strand | A0A225ZZG7 |
| B | 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase (EC 2.1.2.3, 3.5.4.10) | protein | 590 | 43% helix, 18% strand | A0A225ZZG7 |
| C | 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase (EC 2.1.2.3, 3.5.4.10) | protein | 598 | 42% helix, 18% strand | A0A225ZZG7 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1056 | 0.82 | 0.83 | 103 | empty |
| 2 | 1122 | 0.80 | 0.82 | 109 | empty |
| 3 | 119 | 0.78 | 0.97 | 28 | empty |
| 4 | 116 | 0.78 | 0.97 | 28 | empty |
| 5 | 116 | 0.78 | 0.97 | 28 | empty |
Interfaces
3 interfaces between chains.
- C–D · 6916 Ų buried · 103 hydrogen bonds · protein-protein
- A–B · 6727 Ų buried · 104 hydrogen bonds · protein-protein
- A–D · 313 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7MGQ · AICAR transformylase/IMP cyclohydrolase (ATIC) is essential for de novo purine… · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A225ZZG7
- Elsewhere: RCSB PDB 7MGQ · PDBe 7MGQ · UniProt A0A225ZZG7
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