Research workbench
Crystal structure of ankb ankyrin repeats in complex with ANKR/ANKB chimeric autoinhibition segment
Analyse Crystal structure of ankb ankyrin repeats in complex with ANKR/ANKB chimeric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Y4D
- Type
- protein
- Length
- 695 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D3Z5M4, Q01484
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 695 | — | D3Z5M4, Q01484 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 10 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5Y4D · Crystal Structure of AnkB Ankyrin Repeats in Complex with AnkR/AnkB Chimeric… · 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 D3Z5M4
- Every structure of UniProt Q01484
- Elsewhere: RCSB PDB 5Y4D · PDBe 5Y4D · UniProt D3Z5M4 · UniProt Q01484
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