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1Y67

Crystal Structure of Manganese Superoxide Dismutase from Deinococcus radiodurans

Functional Information from GO Data
ChainGOidnamespacecontents
A0004784molecular_functionsuperoxide dismutase activity
A0005737cellular_componentcytoplasm
A0006801biological_processsuperoxide metabolic process
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0046872molecular_functionmetal ion binding
B0004784molecular_functionsuperoxide dismutase activity
B0005737cellular_componentcytoplasm
B0006801biological_processsuperoxide metabolic process
B0016491molecular_functionoxidoreductase activity
B0019430biological_processremoval of superoxide radicals
B0046872molecular_functionmetal ion binding
C0004784molecular_functionsuperoxide dismutase activity
C0005737cellular_componentcytoplasm
C0006801biological_processsuperoxide metabolic process
C0016491molecular_functionoxidoreductase activity
C0019430biological_processremoval of superoxide radicals
C0046872molecular_functionmetal ion binding
D0004784molecular_functionsuperoxide dismutase activity
D0005737cellular_componentcytoplasm
D0006801biological_processsuperoxide metabolic process
D0016491molecular_functionoxidoreductase activity
D0019430biological_processremoval of superoxide radicals
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 229
ChainResidue
AHIS27
AHIS81
AASP173
AHIS177
AHOH233

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B 229
ChainResidue
BHOH230
BHIS27
BHIS81
BASP173
BHIS177

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE C 229
ChainResidue
CHIS27
CHIS81
CASP173
CHIS177
CHOH230

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE D 229
ChainResidue
DHIS27
DHIS81
DASP173
DHIS177
DHOH234

Functional Information from PROSITE/UniProt
site_idPS00088
Number of Residues8
DetailsSOD_MN Manganese and iron superoxide dismutases signature. DvWEHAYY
ChainResidueDetails
AASP173-TYR180

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS28
CSER82
CVAL174
CALA178
DHIS28
DSER82
DVAL174
DALA178
ASER82
AVAL174
AALA178
BHIS28
BSER82
BVAL174
BALA178
CHIS28

222036

PDB entries from 2024-07-03

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