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1IX9

Crystal Structure of the E. coli Manganase(III) superoxide dismutase mutant Y174F at 0.90 angstroms resolution.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0004784molecular_functionsuperoxide dismutase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006801biological_processsuperoxide metabolic process
A0006979biological_processresponse to oxidative stress
A0009408biological_processresponse to heat
A0010447biological_processresponse to acidic pH
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0030145molecular_functionmanganese ion binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0071291biological_processcellular response to selenium ion
B0003677molecular_functionDNA binding
B0004784molecular_functionsuperoxide dismutase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006801biological_processsuperoxide metabolic process
B0006979biological_processresponse to oxidative stress
B0009408biological_processresponse to heat
B0010447biological_processresponse to acidic pH
B0016209molecular_functionantioxidant activity
B0016491molecular_functionoxidoreductase activity
B0019430biological_processremoval of superoxide radicals
B0030145molecular_functionmanganese ion binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0071291biological_processcellular response to selenium ion
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 206
ChainResidue
AHIS26
AHIS81
AASP167
AHIS171
AHOH676

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 206
ChainResidue
BHOH634
BHIS26
BHIS81
BASP167
BHIS171

Functional Information from PROSITE/UniProt
site_idPS00088
Number of Residues8
DetailsSOD_MN Manganese and iron superoxide dismutases signature. DvWEHAYF
ChainResidueDetails
AASP167-PHE174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AHIS27
ASER82
AVAL168
AALA172
BHIS27
BSER82
BVAL168
BALA172

226707

PDB entries from 2024-10-30

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