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Catalytic and structural effects of amino-acid substitution at his 30 in human manganese superoxide dismutase: insertion of val cgamma into the substrate access channel

Analyse Catalytic and structural effects of amino-acid substitution at his 30 in human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1LUV
Type
protein
Length
396 residues
Chains
2
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
Pockets
1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BSuperoxide dismutase [mn] (EC 1.15.1.1)protein19858% helix, 13% strandP04179

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 2 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1600.290.7417empty

Interfaces

1 interface between chains.

  • A–B · 1000 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 1LUV · Catalytic and structural effects of amino-acid substitution at his 30 in human manganese… · the same entry in another collection · chain A against A, TM-score 1.00
  • P04179 · AlphaFold monomer V2.0 prediction for superoxide dismutase [mn], mitochondrial (P04179) · a predicted model of the same protein · chain A against A, TM-score 1.00

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