Research workbench
Crystal structure of phosphoribosylaminoimidazole carboxylase, ATPase subunit from burkholderia ambifaria
Analyse Crystal structure of phosphoribosylaminoimidazole carboxylase, ATPase subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4E4T
- Type
- protein
- Length
- 776 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoribosylaminoimidazole carboxylase, ATPase subunit
- EC
- 4.1.1.21
- UniProt
- B1YVV9
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribosylaminoimidazole carboxylase, ATPase subunit (EC 4.1.1.21) | protein | 391 | 34% helix, 27% strand | B1YVV9 |
| B | Phosphoribosylaminoimidazole carboxylase, ATPase subunit (EC 4.1.1.21) | protein | 385 | 35% helix, 27% strand | B1YVV9 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 352 | 0.85 | 0.94 | 44 | empty |
| 2 | 910 | 0.74 | 0.78 | 72 | SO4 |
| 3 | 544 | 0.65 | 0.77 | 57 | SO4 |
| 4 | 140 | 0.50 | 0.79 | 24 | empty |
| 5 | 153 | 0.47 | 0.77 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 1547 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 4E4T · Crystal structure of Phosphoribosylaminoimidazole carboxylase, ATPase subunit from… · 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 B1YVV9
- Elsewhere: RCSB PDB 4E4T · PDBe 4E4T · UniProt B1YVV9
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