Research workbench
Crystal structure of the dihydroorotase domain of human cad bound to the inhibitor fluoroorotate at pH 7.0
Analyse Crystal structure of the dihydroorotase domain of human cad bound to the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C6M
- Type
- protein
- Length
- 363 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cad protein
- EC
- 3.5.2.3
- UniProt
- P27708
- Ligands
- FOT, ZN
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cad protein (EC 3.5.2.3) | protein | 363 | 36% helix, 20% strand | P27708 |
Ligands and binding sites
- FOT · 5-fluoro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-carboxylic acid · ligand · chains A
- ZN · Zinc ion · metal · 3 copies · chains A
- FMT · Formic acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.58 | 0.81 | 27 | FOT |
| 2 | 73 | 0.40 | 0.78 | 18 | empty |
| 3 | 54 | 0.33 | 0.78 | 17 | FMT |
Modifications
Observed in the structure: 1 modified (carboxylation).
Compared structures
- 4C6M · Crystal structure of the dihydroorotase domain of human CAD bound to the inhibitor… · 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 4C6M · PDBe 4C6M · UniProt P27708
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