Research workbench
Hybrid dihydroorotase domain of human cad with E. COLI flexible loop in apo state
Analyse Hybrid dihydroorotase domain of human cad with E. COLI flexible loop in apo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HG1
- Type
- protein
- Length
- 371 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cad PROTEIN,DIHYDROOROTASE,CAD protein
- EC
- 6.3.5.5, 2.1.3.2, 3.5.2.3
- UniProt
- P27708, P05020
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cad PROTEIN,DIHYDROOROTASE,CAD protein (EC 6.3.5.5, 2.1.3.2, 3.5.2.3) | protein | 371 | 35% helix, 20% strand | P27708, P05020 |
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 | 194 | 0.57 | 0.81 | 28 | empty |
| 2 | 84 | 0.44 | 0.80 | 18 | empty |
| 3 | 54 | 0.32 | 0.77 | 17 | FMT |
Modifications
Observed in the structure: 1 modified (carboxylation).
Compared structures
- 6HG1 · Hybrid dihydroorotase domain of human CAD with E. coli flexible loop in apo state · 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 0.96
- P05020 · AlphaFold monomer V2.0 prediction for dihydroorotase (P05020) · a predicted model of the same protein · chain A against A, TM-score 0.77
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
- Every structure of UniProt P05020
- Elsewhere: RCSB PDB 6HG1 · PDBe 6HG1 · UniProt P27708 · UniProt P05020
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