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The crystal structure of phytoplasmal effector causing phyllody symptoms 1 (PHYL1)
Analyse The crystal structure of phytoplasmal effector causing phyllody symptoms 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6INR
- Type
- protein
- Length
- 144 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative effector, aywb SAP54-like protein
- UniProt
- A0A0P7KHL3
- Ligands
- CD
Structure
x-ray diffraction · 2 distinct chains · 85% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative effector, aywb SAP54-like protein | protein | 75 | 85% helix, 0% strand | A0A0P7KHL3 |
| B | Putative effector, aywb SAP54-like protein | protein | 69 | 86% helix, 0% strand | A0A0P7KHL3 |
Ligands and binding sites
- CD · Cadmium ion · metal · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 610 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 6INR · The crystal structure of phytoplasmal effector causing phyllody symptoms 1 (PHYL1) · 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 A0A0P7KHL3
- Elsewhere: RCSB PDB 6INR · PDBe 6INR · UniProt A0A0P7KHL3
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