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Monomeric human sod mutant F50E/G51E/E133Q at atomic resolution

Analyse Monomeric human sod mutant F50E/G51E/E133Q at atomic resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MFM
Type: protein
Length: 153 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.02
Source: Homo sapiens
Molecule: Protein (COPPER,ZINC superoxide dismutase)
EC: 1.15.1.1
UniProt: P00441
Ligands: CD, ZN, CU, CL

Structure

x-ray diffraction · resolution 1.02 · 1 distinct chain · 5% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (COPPER,ZINC superoxide dismutase) (EC 1.15.1.1)	protein	153	5% helix, 39% strand	P00441

Ligands and binding sites

CD · Cadmium ion · metal · 9 copies · chains A
ZN · Zinc ion · metal · chains A
CU · Copper (II) ion · metal · chains A
CL · Chloride ion · ion · 2 copies · chains A

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

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1MFM · Monomeric human sod mutant F50E/G51E/E133Q at atomic resolution · the same entry in another collection · chain A against A, TM-score 1.00
P00441 · AlphaFold monomer V2.0 prediction for superoxide dismutase [cu-zn] (P00441) · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P00441
Elsewhere: RCSB PDB 1MFM · PDBe 1MFM · UniProt P00441

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