Research workbench
Crystal structure of the catalytic domain of mouse NUDT12 in complex with AMP and 3 MG2+ ions
Analyse Crystal structure of the catalytic domain of mouse NUDT12 in complex with AMP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6O3P
- Type
- protein
- Length
- 628 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9DCN1
- Ligands
- AMP, MG, ZN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 308 | — | Q9DCN1 |
| B | — | protein | 320 | — | Q9DCN1 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 6 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6O3P · Crystal structure of the catalytic domain of mouse Nudt12 in complex with AMP and 3 Mg2+… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9DCN1 · AlphaFold monomer V2.0 prediction for NAD-capped RNA hydrolase NUDT12 (Q9DCN1) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9DCN1
- Elsewhere: RCSB PDB 6O3P · PDBe 6O3P · UniProt Q9DCN1
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