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Crystal structure of orotidine 5'-monophosphate decarboxylase complexed with uridine 5'-monophosphate from P.FALCIPARUM
Analyse Crystal structure of orotidine 5'-monophosphate decarboxylase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZA3
- Type
- protein
- Length
- 631 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Orotidine 5'-phosphate decarboxylase
- EC
- 4.1.1.23
- UniProt
- Q8T6J6
- Ligands
- U5P
- Pockets
- 10 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23) | protein | 315 | 48% helix, 15% strand | Q8T6J6 |
| B | Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23) | protein | 316 | 47% helix, 16% strand | Q8T6J6 |
Ligands and binding sites
- U5P · Uridine-5'-monophosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.78 | 0.96 | 36 | U5P |
| 2 | 128 | 0.77 | 0.95 | 30 | U5P |
| 3 | 114 | 0.42 | 0.77 | 17 | empty |
| 4 | 113 | 0.37 | 0.74 | 17 | empty |
| 5 | 54 | 0.36 | 0.79 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 2526 Ų buried · 38 hydrogen bonds · protein-protein
Compared structures
- 2ZA3 · Crystal Structure of orotidine 5'-monophosphate decarboxylase complexed with uridine… · 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 2ZA3 · PDBe 2ZA3 · UniProt Q8T6J6
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