GL1X · GenesisL1 explorer

Research workbench

Crystal structure of conserved uncharacterized protein from rhodopirellula baltica

Analyse Crystal structure of conserved uncharacterized protein from rhodopirellula… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3B5M
Type
protein
Length
776 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uncharacterized protein
UniProt
Q7UTD8
Ligands
SO4
Pockets
12 · best druggability 0.70

Structure

x-ray diffraction · 3 distinct chains · 34% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUncharacterized proteinprotein19434% helix, 29% strandQ7UTD8
B, DUncharacterized proteinprotein19534% helix, 30% strandQ7UTD8
CUncharacterized proteinprotein19233% helix, 29% strandQ7UTD8

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D

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

Pockets

12 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18420.700.7670empty
22420.650.8334empty
33160.650.8140empty
44300.640.7835SO4
53870.620.7841SO4

Interfaces

4 interfaces between chains.

  • A–B · 1529 Ų buried · 27 hydrogen bonds · protein-protein
  • C–D · 1527 Ų buried · 26 hydrogen bonds · protein-protein
  • B–C · 310 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 274 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 3B5M · Crystal structure of conserved uncharacterized protein from Rhodopirellula baltica · 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.