GL1X · GenesisL1 explorer

Research workbench

Crystal structures of holo and cu-deficient CU/ZNSOD from the silkworm bombyx mori and the implications in amyotrophic lateral sclerosis

Analyse Crystal structures of holo and cu-deficient CU/ZNSOD from the silkworm bombyx… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3L9Y
Type
protein
Length
307 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Superoxide dismutase [cu-zn]
EC
1.15.1.1
UniProt
P82205
Ligands
ZN, CU
Pockets
2 · best druggability 0.55

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASuperoxide dismutase [cu-zn] (EC 1.15.1.1)protein1533% helix, 42% strandP82205
BSuperoxide dismutase [cu-zn] (EC 1.15.1.1)protein1546% helix, 42% strandP82205

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B
  • CU · Copper (II) 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
1570.550.8920empty
22200.460.7432empty

Interfaces

1 interface between chains.

  • A–B · 795 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 3L9Y · Crystal structures of holo and Cu-deficient Cu/ZnSOD from the silkworm Bombyx mori and… · the same entry in another collection · chain A against A, TM-score 1.00
  • P82205 · AlphaFold monomer V2.0 prediction for superoxide dismutase [cu-zn] (P82205) · a predicted model of the same protein · chain B against A, TM-score 0.99

Analyse

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