MolNFT v1 · #75826 · protein
Allosteric regulation by lysine residue: a novel anion-hole formation in the ribokinase family
3Q1Y: “Allosteric regulation by lysine residue: a novel anion-hole formation in the ribokinase family”. X-ray diffraction. MolNFT v1 #75826 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3Q1Y
- Type
- protein
- Length
- 310 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q929S5
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 310 | — | Q929S5 |
Compared structures
- 3Q1Y · Allosteric regulation by Lysine residue: A novel anion-hole formation in the ribokinase… · 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 Q929S5
- Elsewhere: RCSB PDB 3Q1Y · PDBe 3Q1Y · UniProt Q929S5
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