Research workbench
Crystal structure of the effector ECP11-1 from fulvia fulva
Analyse Crystal structure of the effector ECP11-1 from fulvia fulva in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZUS
- Type
- protein
- Length
- 143 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Extracellular protein 11-1
- UniProt
- A0A1P8YXI8
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Extracellular protein 11-1 | protein | 143 | 17% helix, 42% strand | A0A1P8YXI8 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A
- GOL · Glycerol · additive · 4 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 6ZUS · Crystal structure of the effector Ecp11-1 from Fulvia fulva · 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 A0A1P8YXI8
- Elsewhere: RCSB PDB 6ZUS · PDBe 6ZUS · UniProt A0A1P8YXI8
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