MolNFT v1 · #37371 · protein

Crystal structure of hydrophobin hfbi

2FZ6 · Hydrophobin-1: “Crystal structure of hydrophobin hfbi”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.52). MolNFT v1 #37371 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2FZ6
Type: protein
Length: 281 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydrophobin-1
UniProt: P52754
Ligands: ZN
Pockets: 3 · best druggability 0.52

Structure

x-ray diffraction · 4 distinct chains · 12% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydrophobin-1	protein	72	13% helix, 36% strand	P52754
B	Hydrophobin-1	protein	69	12% helix, 39% strand	P52754
C	Hydrophobin-1	protein	71	13% helix, 39% strand	P52754
D	Hydrophobin-1	protein	69	12% helix, 33% strand	P52754

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B, C, D

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

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	204	0.52	0.77	36	empty
2	135	0.41	0.75	27	empty
3	88	0.36	0.75	24	empty

Interfaces

5 interfaces between chains.

C–D · 342 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 318 Å² buried · 3 hydrogen bonds · protein-protein
A–D · 208 Å² buried · 1 hydrogen bond · protein-protein
B–C · 182 Å² buried · 1 hydrogen bond · protein-protein
A–C · 162 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide (disulfide).

Compared structures

2FZ6 · Crystal structure of hydrophobin HFBI · the same entry in another collection · chain D against D, TM-score 1.00
P52754 · AlphaFold monomer V2.0 prediction for hydrophobin-1 (P52754) · a predicted model of the same protein · chain C 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 P52754
Elsewhere: RCSB PDB 2FZ6 · PDBe 2FZ6 · UniProt P52754

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