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Contribution to structure and catalysis of tyrosine 34 in human manganese suerpoxide dismutase

Analyse Contribution to structure and catalysis of tyrosine 34 in human manganese… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ZTE
Type
protein
Length
792 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Superoxide dismutase [mn], mitochondrial
EC
1.15.1.1
UniProt
P04179
Ligands
MN
Pockets
9 · best druggability 0.53

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DSuperoxide dismutase [mn], mitochondrial (EC 1.15.1.1)protein19858% helix, 13% strandP04179

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 4 copies · chains A, B, C, D

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

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11820.530.7923empty
21730.530.7921empty
31830.530.7923empty
42920.520.7436empty
51910.520.7723empty

Interfaces

6 interfaces between chains.

  • C–D · 989 Ų buried · 6 hydrogen bonds · protein-protein
  • A–B · 986 Ų buried · 7 hydrogen bonds · protein-protein
  • A–D · 923 Ų buried · 13 hydrogen bonds · protein-protein
  • B–C · 919 Ų buried · 14 hydrogen bonds · protein-protein
  • A–C · 325 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 1ZTE · Contribution to Structure and Catalysis of Tyrosine 34 in Human Manganese Suerpoxide… · 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

Analyse

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