MolNFT v2 · #152150 · protein
Human dihydroorotase mutant F1563Y co-crystallized with carbamoyl aspartate at pH 6.5
6HFS: “Human dihydroorotase mutant F1563Y co-crystallized with carbamoyl aspartate at pH 6.5”. X-ray diffraction at 1.34905, 2 ligands (NCD, ZN). MolNFT v2 #152150 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6HFS
- Type
- protein
- Length
- 362 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.34905
- Source
- Homo sapiens
- UniProt
- P27708
- Ligands
- NCD, ZN
Structure
x-ray diffraction · resolution 1.34905 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 362 | — | P27708 |
Ligands and binding sites
- NCD · N-carbamoyl-L-aspartate · ligand · chains A
- ZN · Zinc ion · metal · 4 copies · chains A
- FMT · Formic acid · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6HFS · Human dihydroorotase mutant F1563Y co-crystallized with carbamoyl aspartate at pH 6.5 · the same entry in another collection · chain A against A, TM-score 1.00
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 6HFS · PDBe 6HFS · UniProt P27708
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