MolNFT v1 · #63029 · protein
D312N mutant of human orotidyl-5'-monophosphate decarboxylase in complex with 6-azido-ump, covalent adduct
3EX6 · Orotidine-5'-phosphate decarboxylase: “D312N mutant of human orotidyl-5'-monophosphate decarboxylase in complex with 6-azido-ump, covalent adduct”. X-ray diffraction, 3 ligands (U5P, SO4, CL), 5 pockets (best druggability 0.74).…
- PDB
- 3EX6
- Type
- protein
- Length
- 514 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
- P11172
- Ligands
- U5P, SO4, CL
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) | protein | 257 | 44% helix, 18% strand | P11172 |
Ligands and binding sites
- U5P · Uridine-5'-monophosphate · ligand · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A, B
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 101 | 0.74 | 0.95 | 28 | SO4, CL |
| 2 | 103 | 0.73 | 0.95 | 29 | U5P |
| 3 | 56 | 0.34 | 0.78 | 19 | empty |
| 4 | 56 | 0.33 | 0.77 | 16 | empty |
| 5 | 50 | 0.32 | 0.78 | 13 | GOL |
Interfaces
1 interface between chains.
- A–B · 1925 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 3EX6 · D312N mutant of human orotidyl-5'-monophosphate decarboxylase in complex with… · 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 P11172
- Elsewhere: RCSB PDB 3EX6 · PDBe 3EX6 · UniProt P11172
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