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1ISA

STRUCTURE-FUNCTION IN E. COLI IRON SUPEROXIDE DISMUTASE: COMPARISONS WITH THE MANGANESE ENZYME FROM T. THERMOPHILUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000303biological_processresponse to superoxide
A0004784molecular_functionsuperoxide dismutase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006801biological_processsuperoxide metabolic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0046872molecular_functionmetal ion binding
B0000303biological_processresponse to superoxide
B0004784molecular_functionsuperoxide dismutase activity
B0005506molecular_functioniron ion binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006801biological_processsuperoxide metabolic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0019430biological_processremoval of superoxide radicals
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 193
ChainResidue
AHIS26
AHIS73
AASP156
AHIS160
AHOH194

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 B 193
ChainResidue
BHIS26
BHIS73
BASP156
BHIS160
BHOH194

site_idFEA
Number of Residues5
Details
ChainResidue
AHIS26
AHIS73
AASP156
AHIS160
AHOH194

site_idFEB
Number of Residues5
Details
ChainResidue
BHOH194
BHIS26
BHIS73
BASP156
BHIS160

Functional Information from PROSITE/UniProt
site_idPS00088
Number of Residues8
DetailsSOD_MN Manganese and iron superoxide dismutases signature. DvWEHAYY
ChainResidueDetails
AASP156-TYR163

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ATYR27
ATHR74
AVAL157
AALA161
BTYR27
BTHR74
BVAL157
BALA161

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ASER51
BSER51

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PDB entries from 2024-10-02

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