Research workbench
Orhorhombic crystal structure of hydrophobin hfbii in the presence of a detergent
Analyse Orhorhombic crystal structure of hydrophobin hfbii in the presence of a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PL7
- Type
- protein
- Length
- 134 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydrophobin-2
- UniProt
- P79073
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Hydrophobin-2 | protein | 67 | 13% helix, 42% strand | P79073 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains B
- HTG · heptyl 1-thio-beta-D-glucopyranoside · additive · 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 · 473 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 2PL7 · Orhorhombic crystal structure of hydrophobin HFBII in the presence of a detergent · the same entry in another collection · chain A against A, TM-score 1.00
- P79073 · AlphaFold monomer V2.0 prediction for hydrophobin-2 (P79073) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P79073
- Elsewhere: RCSB PDB 2PL7 · PDBe 2PL7 · UniProt P79073
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