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2JLP

Crystal structure of human extracellular copper-zinc superoxide dismutase.

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0004784molecular_functionsuperoxide dismutase activity
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005794cellular_componentGolgi apparatus
A0005796cellular_componentGolgi lumen
A0006801biological_processsuperoxide metabolic process
A0006979biological_processresponse to oxidative stress
A0008201molecular_functionheparin binding
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0046688biological_processresponse to copper ion
A0046872molecular_functionmetal ion binding
A0060090molecular_functionmolecular adaptor activity
A0062023cellular_componentcollagen-containing extracellular matrix
A0070062cellular_componentextracellular exosome
A0097746biological_processblood vessel diameter maintenance
B0001666biological_processresponse to hypoxia
B0004784molecular_functionsuperoxide dismutase activity
B0005507molecular_functioncopper ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005794cellular_componentGolgi apparatus
B0005796cellular_componentGolgi lumen
B0006801biological_processsuperoxide metabolic process
B0006979biological_processresponse to oxidative stress
B0008201molecular_functionheparin binding
B0016209molecular_functionantioxidant activity
B0016491molecular_functionoxidoreductase activity
B0019430biological_processremoval of superoxide radicals
B0046688biological_processresponse to copper ion
B0046872molecular_functionmetal ion binding
B0060090molecular_functionmolecular adaptor activity
B0062023cellular_componentcollagen-containing extracellular matrix
B0070062cellular_componentextracellular exosome
B0097746biological_processblood vessel diameter maintenance
C0001666biological_processresponse to hypoxia
C0004784molecular_functionsuperoxide dismutase activity
C0005507molecular_functioncopper ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005794cellular_componentGolgi apparatus
C0005796cellular_componentGolgi lumen
C0006801biological_processsuperoxide metabolic process
C0006979biological_processresponse to oxidative stress
C0008201molecular_functionheparin binding
C0016209molecular_functionantioxidant activity
C0016491molecular_functionoxidoreductase activity
C0019430biological_processremoval of superoxide radicals
C0046688biological_processresponse to copper ion
C0046872molecular_functionmetal ion binding
C0060090molecular_functionmolecular adaptor activity
C0062023cellular_componentcollagen-containing extracellular matrix
C0070062cellular_componentextracellular exosome
C0097746biological_processblood vessel diameter maintenance
D0001666biological_processresponse to hypoxia
D0004784molecular_functionsuperoxide dismutase activity
D0005507molecular_functioncopper ion binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005794cellular_componentGolgi apparatus
D0005796cellular_componentGolgi lumen
D0006801biological_processsuperoxide metabolic process
D0006979biological_processresponse to oxidative stress
D0008201molecular_functionheparin binding
D0016209molecular_functionantioxidant activity
D0016491molecular_functionoxidoreductase activity
D0019430biological_processremoval of superoxide radicals
D0046688biological_processresponse to copper ion
D0046872molecular_functionmetal ion binding
D0060090molecular_functionmolecular adaptor activity
D0062023cellular_componentcollagen-containing extracellular matrix
D0070062cellular_componentextracellular exosome
D0097746biological_processblood vessel diameter maintenance
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A 225
ChainResidue
AHIS96
AHIS98
AHIS113
AHIS163
AHOH2128

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 226
ChainResidue
AHIS113
AHIS121
AHIS124
AASP127

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU B 225
ChainResidue
BHIS96
BHIS98
BHIS113
BHIS163
BSCN227

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 226
ChainResidue
BHIS113
BHIS121
BHIS124
BASP127

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SCN B 227
ChainResidue
BHIS98
BPRO112
BHIS113
BHIS163
BASN180
BARG186
BCU225
BHOH2195
BHOH2208
BHOH2223

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU C 225
ChainResidue
CHIS96
CHIS98
CHIS113
CHIS163
CSCN227

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 226
ChainResidue
CHIS113
CHIS121
CHIS124
CASP127

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SCN C 227
ChainResidue
CHIS98
CPRO112
CHIS113
CHIS163
CASN180
CARG186
CCU225
CHOH2193
CHOH2197
CHOH2203
CHOH2214
CHOH2215

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU D 225
ChainResidue
DHIS96
DHIS98
DHIS113
DHIS163
DHOH2114

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 226
ChainResidue
DHIS113
DHIS121
DHIS124
DASP127

Functional Information from PROSITE/UniProt
site_idPS00087
Number of Residues11
DetailsSOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. AIHVHQfGDlS
ChainResidueDetails
AALA94-SER104

site_idPS00332
Number of Residues12
DetailsSOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGrRlACcvV
ChainResidueDetails
AGLY181-VAL192

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBINDING:
ChainResidueDetails
AHIS96
AHIS98
BASP127
BHIS163
CHIS96
CHIS98
CHIS113
CHIS121
CHIS124
CASP127
CHIS163
DHIS96
DHIS98
DHIS113
DHIS121
DHIS124
DASP127
DHIS163
AHIS113
AHIS121
AHIS124
AASP127
AHIS163
BHIS96
BHIS98
BHIS113
BHIS121
BHIS124

site_idSWS_FT_FI2
Number of Residues12
DetailsSITE: Not glycated
ChainResidueDetails
ALYS23
ALYS74
ALYS220
BLYS23
BLYS74
BLYS220
CLYS23
CLYS74
CLYS220
DLYS23
DLYS74
DLYS220

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN89
BASN89
CASN89
DASN89

site_idSWS_FT_FI4
Number of Residues8
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:1505778
ChainResidueDetails
CLYS211
CLYS212
DLYS211
DLYS212
ALYS211
ALYS212
BLYS211
BLYS212

221051

PDB entries from 2024-06-12

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