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Crystal structure of plasmodium falciparum orotidine 5'-phosphate decarboxylase covalently modified by 6-iodo-ump
Analyse Crystal structure of plasmodium falciparum orotidine 5'-phosphate decarboxylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QAF
- Type
- protein
- Length
- 651 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Orotidine 5' monophosphate decarboxylase
- EC
- 4.1.1.23
- UniProt
- Q8T6J6
- Ligands
- U5P, SO4
- Pockets
- 8 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Orotidine 5' monophosphate decarboxylase (EC 4.1.1.23) | protein | 329 | 56% helix, 15% strand | Q8T6J6 |
| B | Orotidine 5' monophosphate decarboxylase (EC 4.1.1.23) | protein | 322 | 54% helix, 16% strand | Q8T6J6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.72 | 0.96 | 22 | U5P |
| 2 | 82 | 0.72 | 0.96 | 31 | U5P |
| 3 | 123 | 0.45 | 0.77 | 19 | empty |
| 4 | 143 | 0.44 | 0.76 | 15 | empty |
| 5 | 130 | 0.43 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2525 Ų buried · 31 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 2QAF · Crystal structure of Plasmodium falciparum orotidine 5'-phosphate decarboxylase… · 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 Q8T6J6
- Elsewhere: RCSB PDB 2QAF · PDBe 2QAF · UniProt Q8T6J6
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