MolNFT v1 · #138192 · protein

Peroxide activation regulated by hydrogen bonds within artificial cu proteins - S112A

5WBB · Streptavidin: “Peroxide activation regulated by hydrogen bonds within artificial cu proteins - S112A”. X-ray diffraction, 3 ligands (SQ1, CU, SO4), 1 pocket (best druggability 0.48). MolNFT v1 #138192 on GenesisL1: 3D structure…

PDB: 5WBB
Type: protein
Length: 125 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Streptavidin
UniProt: P22629
Ligands: SQ1, CU, SO4
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Streptavidin	protein	125	8% helix, 54% strand	P22629

Ligands and binding sites

SQ1 · [N-(2-{bis[2-(pyridin-2-yl-kappaN)ethyl]amino-kappaN}ethyl)-5-(2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamide]copper · ligand · chains A
CU · Copper (II) ion · metal · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · chains A

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	94	0.48	0.81	17	SQ1

Compared structures

5WBB · Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins - S112A · 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 P22629
Elsewhere: RCSB PDB 5WBB · PDBe 5WBB · UniProt P22629

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