GL1X · GenesisL1 explorer

Research workbench

Crystal structure of bovine cu, zn sod to 1.7 ångström (3 of 3)

Analyse Crystal structure of bovine cu, zn sod to 1.7 ångström (3 of 3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1E9P
Type
protein
Length
302 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Superoxide dismutase
EC
1.13.1.1
UniProt
P00442
Ligands
CU, ZN
Pockets
2 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASuperoxide dismutase (EC 1.13.1.1)protein1516% helix, 42% strandP00442
BSuperoxide dismutase (EC 1.13.1.1)protein1516% helix, 42% strandP00442

Ligands and binding sites

  • CU · Copper (II) ion · metal · 3 copies · chains A, B
  • ZN · Zinc ion · metal · chains 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
11860.570.8133empty
2980.360.7518empty

Interfaces

1 interface between chains.

  • A–B · 653 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 1E9P · Crystal structure of bovine Cu, Zn SOD to 1.7 Angstrom (3 of 3) · the same entry in another collection · chain A against A, TM-score 1.00
  • P00442 · AlphaFold monomer V2.0 prediction for superoxide dismutase [cu-zn] (P00442) · a predicted model of the same protein · 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.