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7YPR

Structural basis of a superoxide dismutase from a tardigrade, Ramazzottius varieornatus strain YOKOZUNA-1.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0006801biological_processsuperoxide metabolic process
A0046872molecular_functionmetal ion binding
B0005507molecular_functioncopper ion binding
B0006801biological_processsuperoxide metabolic process
B0046872molecular_functionmetal ion binding
C0005507molecular_functioncopper ion binding
C0006801biological_processsuperoxide metabolic process
C0046872molecular_functionmetal ion binding
D0005507molecular_functioncopper ion binding
D0006801biological_processsuperoxide metabolic process
D0046872molecular_functionmetal ion binding
E0005507molecular_functioncopper ion binding
E0006801biological_processsuperoxide metabolic process
E0046872molecular_functionmetal ion binding
F0005507molecular_functioncopper ion binding
F0006801biological_processsuperoxide metabolic process
F0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00332
Number of Residues12
DetailsSOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGgRlACgiI
ChainResidueDetails
AGLY180-ILE191

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBINDING: BINDING => ECO:0000269|PubMed:37358501, ECO:0007744|PDB:7YPP, ECO:0007744|PDB:7YPR
ChainResidueDetails
AHIS85
BHIS121
BASP124
BHIS162
CHIS85
CHIS104
CHIS112
CHIS121
CASP124
CHIS162
DHIS85
AHIS104
DHIS104
DHIS112
DHIS121
DASP124
DHIS162
EHIS85
EHIS104
EHIS112
EHIS121
EASP124
AHIS112
EHIS162
FHIS85
FHIS104
FHIS112
FHIS121
FASP124
FHIS162
AHIS121
AASP124
AHIS162
BHIS85
BHIS104
BHIS112

223532

PDB entries from 2024-08-07

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