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Crystal structure of human MORC2 (residues 1-603) with spinal muscular atrophy mutation T424R
Analyse Crystal structure of human MORC2 (residues 1-603) with spinal muscular atrophy… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OFA
- Type
- protein
- Length
- 1,071 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9Y6X9
- Ligands
- ANP, ZN, MG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 540 | — | Q9Y6X9 |
| A | — | protein | 531 | — | Q9Y6X9 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains B, A
- ZN · Zinc ion · metal · 2 copies · chains B, A
- MG · Magnesium ion · metal · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OFA · Crystal structure of human MORC2 (residues 1-603) with spinal muscular atrophy mutation… · the same entry in another collection · chain B against B, TM-score 1.00
- Q9Y6X9 · AlphaFold monomer V2.0 prediction for ATPase MORC2 (Q9Y6X9) · a predicted model of the same protein · chain A 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 Q9Y6X9
- Elsewhere: RCSB PDB 5OFA · PDBe 5OFA · UniProt Q9Y6X9
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