GL1X · GenesisL1 explorer

Research workbench

Crystal structure of protein yfih from shigella flexneri, pfam DUF152

Analyse Crystal structure of protein yfih from shigella flexneri, pfam DUF152 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1U05
Type
protein
Length
486 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Orf, conserved hypothetical protein
UniProt
Q83K13
Ligands
ZN
Pockets
2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BOrf, conserved hypothetical proteinprotein24324% helix, 27% strandQ83K13

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19970.800.8188ZN
21910.500.7628ZN

Interfaces

1 interface between chains.

  • A–B · 599 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 1U05 · Crystal structure of protein yfiH from Shigella flexneri, Pfam DUF152 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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