Research workbench
Human dihydroorotase mutant F1563Y co-crystallized with carbamoyl aspartate at pH 6.5
Analyse Human dihydroorotase mutant F1563Y co-crystallized with carbamoyl aspartate at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HFS
- Type
- protein
- Length
- 362 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.34905
- Source
- Homo sapiens
- Molecule
- CAD protein
- EC
- 6.3.5.5, 2.1.3.2, 3.5.2.3
- UniProt
- P27708
- Ligands
- NCD, ZN
- Pockets
- 2 · best druggability 0.39
Structure
x-ray diffraction · resolution 1.34905 · 1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CAD protein (EC 6.3.5.5, 2.1.3.2, 3.5.2.3) | protein | 362 | 36% helix, 20% strand | P27708 |
Ligands and binding sites
- NCD · N-carbamoyl-L-aspartate · ligand · chains A
- ZN · Zinc ion · metal · 4 copies · chains A
- FMT · Formic acid · additive · 3 copies · chains A
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 | 80 | 0.39 | 0.77 | 16 | empty |
| 2 | 55 | 0.32 | 0.77 | 17 | FMT |
Modifications
Observed in the structure: 1 modified (carboxylation).
Compared structures
- 6HFS · Human dihydroorotase mutant F1563Y co-crystallized with carbamoyl aspartate at pH 6.5 · the same entry in another collection · chain A against A, TM-score 1.00
- P27708 · AlphaFold monomer V2.0 prediction for cad protein (P27708) · a predicted model of the same protein · chain A 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 P27708
- Elsewhere: RCSB PDB 6HFS · PDBe 6HFS · UniProt P27708
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