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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1JK9

Heterodimer between H48F-ySOD1 and yCCS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004784molecular_functionsuperoxide dismutase activity
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005758cellular_componentmitochondrial intermembrane space
A0005829cellular_componentcytosol
A0006801biological_processsuperoxide metabolic process
A0006825biological_processcopper ion transport
A0006878biological_processintracellular copper ion homeostasis
A0006882biological_processintracellular zinc ion homeostasis
A0008270molecular_functionzinc ion binding
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0016670molecular_functionoxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor
A0019430biological_processremoval of superoxide radicals
A0031505biological_processfungal-type cell wall organization
A0034599biological_processcellular response to oxidative stress
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046872molecular_functionmetal ion binding
A0050821biological_processprotein stabilization
A1901856biological_processnegative regulation of cellular respiration
A1902693cellular_componentsuperoxide dismutase complex
A1990748biological_processcellular detoxification
B0005507molecular_functioncopper ion binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005758cellular_componentmitochondrial intermembrane space
B0005829cellular_componentcytosol
B0006801biological_processsuperoxide metabolic process
B0006825biological_processcopper ion transport
B0016532molecular_functionsuperoxide dismutase copper chaperone activity
B0019430biological_processremoval of superoxide radicals
B0046872molecular_functionmetal ion binding
B0101031cellular_componentprotein folding chaperone complex
B1902693cellular_componentsuperoxide dismutase complex
C0004784molecular_functionsuperoxide dismutase activity
C0005507molecular_functioncopper ion binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005758cellular_componentmitochondrial intermembrane space
C0005829cellular_componentcytosol
C0006801biological_processsuperoxide metabolic process
C0006825biological_processcopper ion transport
C0006878biological_processintracellular copper ion homeostasis
C0006882biological_processintracellular zinc ion homeostasis
C0008270molecular_functionzinc ion binding
C0016209molecular_functionantioxidant activity
C0016491molecular_functionoxidoreductase activity
C0016670molecular_functionoxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor
C0019430biological_processremoval of superoxide radicals
C0031505biological_processfungal-type cell wall organization
C0034599biological_processcellular response to oxidative stress
C0045944biological_processpositive regulation of transcription by RNA polymerase II
C0046872molecular_functionmetal ion binding
C0050821biological_processprotein stabilization
C1901856biological_processnegative regulation of cellular respiration
C1902693cellular_componentsuperoxide dismutase complex
C1990748biological_processcellular detoxification
D0005507molecular_functioncopper ion binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005743cellular_componentmitochondrial inner membrane
D0005758cellular_componentmitochondrial intermembrane space
D0005829cellular_componentcytosol
D0006801biological_processsuperoxide metabolic process
D0006825biological_processcopper ion transport
D0016532molecular_functionsuperoxide dismutase copper chaperone activity
D0019430biological_processremoval of superoxide radicals
D0046872molecular_functionmetal ion binding
D0101031cellular_componentprotein folding chaperone complex
D1902693cellular_componentsuperoxide dismutase complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS63
AHIS71
AHIS80
AASP83
site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 302
ChainResidue
CHIS63
CHIS71
CHIS80
CASP83
site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 303
ChainResidue
CGLU42
DHIS198
DGLU200
BHIS16
site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 304
ChainResidue
AGLU42
BHIS198
BGLU200
DHIS16
site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
APHE48
AHIS120
AARG143
BLYS226
BCYS229
BALA230
site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 402
ChainResidue
CPHE48
CARG143
DLYS226
DCYS229
DALA230
Functional Information from PROSITE/UniProt
site_idPS00332
Number of Residues12
DetailsSOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGpRpACgvI
ChainResidueDetails
AGLY138-ILE149
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"description":"in apo form","evidences":[{"source":"PubMed","id":"10026301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11524675","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10026301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8652572","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10026301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11524675","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15665377","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"PubMed","id":"15166219","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues126
DetailsDomain: {"description":"HMA","evidences":[{"source":"PROSITE-ProRule","id":"PRU00280","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11524675","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JK9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00280","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
AARG143
AHIS63
site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
CARG143
CHIS63
site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
AHIS63
site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
CHIS63
site_idMCSA1
Number of Residues8
DetailsM-CSA 138
ChainResidueDetails
AHIS46metal ligand
APHE48metal ligand
AHIS63hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
AHIS71metal ligand
AHIS80metal ligand
AASP83metal ligand
AHIS120metal ligand
AARG143electrostatic stabiliser, hydrogen bond donor
site_idMCSA2
Number of Residues8
DetailsM-CSA 138
ChainResidueDetails
CHIS46metal ligand
CPHE48metal ligand
CHIS63hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
CHIS71metal ligand
CHIS80metal ligand
CASP83metal ligand
CHIS120metal ligand
CARG143electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2025-07-09

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