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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1B4T

H48C YEAST CU(II)/ZN SUPEROXIDE DISMUTASE ROOM TEMPERATURE (298K) STRUCTURE

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A 154
ChainResidue
AHIS46
AHIS63
AHIS120
ACL156
AHOH201
site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 155
ChainResidue
AHIS63
AHIS71
AHIS80
AASP83
ALYS136
site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 156
ChainResidue
AHIS63
AHIS120
AARG143
ACU154
site_idCU
Number of Residues5
DetailsCOPPER BINDING SITE
ChainResidue
ACU154
AHIS46
AHIS63
AHIS120
ACL156
site_idZN
Number of Residues5
DetailsZINC BINDING SITE
ChainResidue
AASP83
AZN155
AHIS63
AHIS71
AHIS80
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 Residues1
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 Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10026301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8652572","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10026301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11524675","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
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 Residues1
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 Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"PubMed","id":"15166219","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
AARG143
AHIS63
site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
AHIS63
site_idMCSA1
Number of Residues8
DetailsM-CSA 138
ChainResidueDetails
AHIS46metal ligand
ACYS48metal 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

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PDB entries from 2025-11-05

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