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1XSO

THREE-DIMENSIONAL STRUCTURE OF XENOPUS LAEVIS CU,ZN SUPEROXIDE DISMUTASE B DETERMINED BY X-RAY CRYSTALLOGRAPHY AT 1.5 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004784molecular_functionsuperoxide dismutase activity
A0005507molecular_functioncopper ion binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0006801biological_processsuperoxide metabolic process
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
B0004784molecular_functionsuperoxide dismutase activity
B0005507molecular_functioncopper ion binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005777cellular_componentperoxisome
B0005829cellular_componentcytosol
B0006801biological_processsuperoxide metabolic process
B0016209molecular_functionantioxidant activity
B0016491molecular_functionoxidoreductase activity
B0019430biological_processremoval of superoxide radicals
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idA
Number of Residues9
Details
ChainResidue
AHIS44
AHIS46
AHIS61
AHIS118
AHIS69
AHIS78
AASP81
ACU1
AZN152

site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A 1
ChainResidue
AHIS44
AHIS46
AHIS61
AHIS118
AHOH167

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 152
ChainResidue
AHIS61
AHIS69
AHIS78
AASP81

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CU B 152
ChainResidue
BHIS44
BHIS46
BHIS61
BHIS118
BHOH154
BHOH159

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 153
ChainResidue
BHIS61
BHIS69
BHIS78
BASP81

site_idB
Number of Residues9
Details
ChainResidue
BHIS44
BHIS46
BHIS61
BHIS118
BHIS69
BHIS78
BASP81
BCU152
BZN153

Functional Information from PROSITE/UniProt
site_idPS00087
Number of Residues11
DetailsSOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. GFHIHVfGDnT
ChainResidueDetails
AGLY42-THR52

site_idPS00332
Number of Residues12
DetailsSOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGgRlACgvI
ChainResidueDetails
AGLY136-ILE147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING:
ChainResidueDetails
AILE45
BPHE62
BGLY70
BVAL79
BLEU82
BGLU119
AVAL47
APHE62
AGLY70
AVAL79
ALEU82
AGLU119
BILE45
BVAL47

site_idSWS_FT_FI2
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250
ChainResidueDetails
AVAL7
BVAL7

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
AHIS61
AARG141

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
BHIS61
BARG141

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
AHIS61

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
BHIS61

226707

PDB entries from 2024-10-30

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