GL1X · GenesisL1 explorer

Research workbench

Human manganese superoxide dismutase

Analyse Human manganese superoxide dismutase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ADQ
Type
protein
Length
196 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Superoxide dismutase [mn]
EC
1.15.1.1
UniProt
P04179
Ligands
MN, K

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BSuperoxide dismutase [mn] (EC 1.15.1.1)protein19657% helix, 13% strandP04179

Ligands and binding sites

  • MN · Manganese (II) ion · metal · chains B
  • K · Potassium ion · metal · chains B

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

Compared structures

  • 2ADQ · Human Manganese Superoxide Dismutase · the same entry in another collection · chain B against B, TM-score 1.00
  • P04179 · AlphaFold monomer V2.0 prediction for superoxide dismutase [mn], mitochondrial (P04179) · a predicted model of the same protein · chain B 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.