Research workbench
AVR2 effector protein from the fungal plant pathogen fusarium oxysporum
Analyse AVR2 effector protein from the fungal plant pathogen fusarium oxysporum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OD4
- Type
- protein
- Length
- 124 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Secreted in xylem 3
- UniProt
- Q2A0P1
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Secreted in xylem 3 | protein | 124 | 2% helix, 43% strand | Q2A0P1 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5OD4 · Avr2 effector protein from the fungal plant pathogen Fusarium oxysporum · 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 Q2A0P1
- Elsewhere: RCSB PDB 5OD4 · PDBe 5OD4 · UniProt Q2A0P1
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