MolNFT v1 · #138191 · protein

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

5WBA · Streptavidin: “Peroxide activation regulated by hydrogen bonds within artificial cu proteins - wt”. X-ray diffraction, 3 ligands (SI8, CU, SO4), 1 pocket (best druggability 0.48). MolNFT v1 #138191 on GenesisL1: 3D structure…

PDB: 5WBA
Type: protein
Length: 125 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Streptavidin
UniProt: P22629
Ligands: SI8, CU, SO4
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Streptavidin	protein	125	6% helix, 54% strand	P22629

Ligands and binding sites

SI8 · [N-(2-{bis[2-(pyridin-2-yl-kappaN)ethyl]amino-kappaN}ethyl)-5-(2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamide](hydrogen peroxido-kappaO)copper · ligand · chains A
CU · Copper (II) ion · metal · chains A
SO4 · Sulfate ion · ion · chains A
ACT · Acetate ion · 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	93	0.48	0.81	17	SI8

Compared structures

5WBA · Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins - WT · 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 5WBA · PDBe 5WBA · UniProt P22629

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