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Crystal structure of the zuotin homology domain (ZHD) from yeast Zuo1
Analyse Crystal structure of the zuotin homology domain (ZHD) from yeast Zuo1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DJE
- Type
- protein
- Length
- 271 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.85
- Source
- Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
- Molecule
- Zuotin
- UniProt
- P32527
Structure
x-ray diffraction · resolution 1.85 · 2 distinct chains · 58% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zuotin | protein | 135 | 59% helix, 1% strand | P32527 |
| B | Zuotin | protein | 136 | 57% helix, 1% strand | P32527 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
- BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · chains B
- EDO · 1,2-ethanediol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
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 P32527
- Elsewhere: RCSB PDB 5DJE · PDBe 5DJE · UniProt P32527
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