Research workbench
Structural basis for allosteric substrate specificity regulation in class III ribonucleotide reductases: nrdd in complex with datp
Analyse Structural basis for allosteric substrate specificity regulation in class III… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H7A
- Type
- protein
- Length
- 563 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9T0V5
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 563 | — | Q9T0V5 |
Compared structures
- 1H7A · Structural basis for allosteric substrate specificity regulation in class III… · 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 Q9T0V5
- Elsewhere: RCSB PDB 1H7A · PDBe 1H7A · UniProt Q9T0V5
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