Research workbench
Crystal structure of orotate phosphoribosyltransferase from streptococcus pyogenes
Analyse Crystal structure of orotate phosphoribosyltransferase from streptococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AEE
- Type
- protein
- Length
- 409 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Orotate phosphoribosyltransferase
- EC
- 2.4.2.10
- UniProt
- Q9A076
- Ligands
- SO4, CL
- Pockets
- 2 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Orotate phosphoribosyltransferase (EC 2.4.2.10) | protein | 206 | 46% helix, 21% strand | Q9A076 |
| B | Orotate phosphoribosyltransferase (EC 2.4.2.10) | protein | 203 | 45% helix, 23% strand | Q9A076 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- CL · Chloride ion · ion · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 211 | 0.47 | 0.74 | 32 | SO4, GOL |
| 2 | 170 | 0.44 | 0.75 | 32 | SO4, GOL |
Interfaces
1 interface between chains.
- A–B · 1352 Ų buried · 29 hydrogen bonds · protein-protein
Compared structures
- 2AEE · Crystal structure of Orotate phosphoribosyltransferase from Streptococcus pyogenes · the same entry in another collection · chain A against A, TM-score 1.00
- Q9A076 · AlphaFold monomer V2.0 prediction for orotate phosphoribosyltransferase (Q9A076) · a predicted model of the same protein · chain B 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 Q9A076
- Elsewhere: RCSB PDB 2AEE · PDBe 2AEE · UniProt Q9A076
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