MolNFT v1 · #87621 · protein
Crystal structure of the dihydroorotase domain of human cad C1613S mutant in apo-form at pH 7.0
4C6P · Cad protein: “Crystal structure of the dihydroorotase domain of human cad C1613S mutant in apo-form at pH 7.0”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.59). MolNFT v1 #87621 on GenesisL1: 3D structure…
- PDB
- 4C6P
- Type
- protein
- Length
- 362 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
- ZN
- Pockets
- 3 · best druggability 0.59
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 | 362 | 36% helix, 20% strand | P27708 |
Ligands and binding sites
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 | 201 | 0.59 | 0.81 | 28 | FMT |
| 2 | 66 | 0.38 | 0.78 | 16 | empty |
| 3 | 54 | 0.30 | 0.76 | 17 | FMT |
Modifications
Observed in the structure: 1 modified (carboxylation).
Compared structures
- 4C6P · Crystal structure of the dihydroorotase domain of human CAD C1613S mutant in apo-form at… · 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 4C6P · PDBe 4C6P · UniProt P27708
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