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Crystal structure of beta hordothionin

Analyse Crystal structure of beta hordothionin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WUW
Type: protein
Length: 90 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-hordothionin
UniProt: P21742
Ligands: TSU, SER
Pockets: 1 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Beta-hordothionin	protein	45	40% helix, 9% strand	P21742

Ligands and binding sites

TSU · Para-toluene sulfonate · ligand · 2 copies · chains A, B
SER · Serine · ligand · 2 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	116	0.46	0.79	18	TSU

Interfaces

1 interface between chains.

A–B · 484 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

1WUW · Crystal Structure of beta hordothionin · the same entry in another collection · chain A against A, TM-score 1.00
P21742 · AlphaFold monomer V2.0 prediction for beta-hordothionin (P21742) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P21742
Elsewhere: RCSB PDB 1WUW · PDBe 1WUW · UniProt P21742

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