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Ultra-high resolution structure of hydrophobin hfbii

Analyse Ultra-high resolution structure of hydrophobin hfbii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2B97
Type: protein
Length: 140 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydrophobin II
UniProt: P79073
Ligands: MN

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hydrophobin II	protein	70	14% helix, 40% strand	P79073

Ligands and binding sites

MN · Manganese (II) ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

A–B · 300 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

2B97 · Ultra-high resolution structure of hydrophobin HFBII · 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 0.94

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 2B97 · PDBe 2B97 · UniProt P79073

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