Research workbench
Hybrid dihydroorotase domain of human cad with E. COLI flexible loop, bound to fluoroorotate
Analyse Hybrid dihydroorotase domain of human cad with E. COLI flexible loop, bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 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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