MolNFT v1 · #21788 · protein

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

1SLF: “Apostreptavidin, pH 5.6, two molecules of (SO4)2 bound at the biotin binding site”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.48). MolNFT v1 #21788 on GenesisL1: 3D structure, binding sites and pockets in…

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.