Research workbench

Apostreptavidin, pH 5.6, two molecules of (SO4)2 bound at the biotin binding site

Analyse Apostreptavidin, pH 5.6, two molecules of (SO4)2 bound at the biotin binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SLF
Type: protein
Length: 244 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Streptavidin
UniProt: P22629
Ligands: SO4
Pockets: 3 · best druggability 0.48

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Streptavidin	protein	123	8% helix, 55% strand	P22629
D	Streptavidin	protein	121	8% helix, 56% strand	P22629

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains B, 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	90	0.48	0.81	17	SO4
2	91	0.46	0.80	17	SO4
3	76	0.32	0.75	21	empty

Interfaces

1 interface between chains.

B–D · 1595 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

1SLF · Apostreptavidin, pH 5.6, two molecules of (SO4)2 bound at the biotin binding site · the same entry in another collection · chain B against B, 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 1SLF · PDBe 1SLF · UniProt P22629

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.