MolNFT v1 · #151186 · protein
Hybrid dihydroorotase domain of human cad with E. COLI flexible loop, bound to fluoroorotate
6HG2 · Cad protein: “Hybrid dihydroorotase domain of human cad with E. COLI flexible loop, bound to fluoroorotate”. X-ray diffraction, 2 ligands (FOT, ZN), 3 pockets (best druggability 0.50). MolNFT v1 #151186 on GenesisL1: 3D structure…
- PDB
- 6HG2
- Type
- protein
- Length
- 356 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cad protein
- EC
- 6.3.5.5, 2.1.3.2, 3.5.2.3
- UniProt
- P27708
- Ligands
- FOT, ZN
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 21% 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 | 356 | 35% helix, 21% 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 · 2 copies · chains A
- FMT · Formic acid · additive · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 169 | 0.50 | 0.78 | 33 | ZN, FOT |
| 2 | 58 | 0.37 | 0.79 | 14 | empty |
| 3 | 59 | 0.32 | 0.76 | 18 | empty |
Modifications
Observed in the structure: 1 modified (carboxylation).
Compared structures
- 6HG2 · Hybrid dihydroorotase domain of human CAD with E. coli flexible loop, bound to… · 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 6HG2 · PDBe 6HG2 · UniProt P27708
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