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1YSO

YEAST CU, ZN SUPEROXIDE DISMUTASE WITH THE REDUCED BRIDGE BROKEN

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
A0006878biological_processintracellular copper ion homeostasis
A0006882biological_processintracellular zinc ion homeostasis
A0008270molecular_functionzinc ion binding
A0015680biological_processprotein maturation by copper ion transfer
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 Residues4
DetailsBINDING SITE FOR RESIDUE CU1 A 154
ChainResidue
AHIS46
AHIS48
AHIS63
AHIS120

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 155
ChainResidue
AHIS63
AHIS71
AHIS80
AASP83

site_idCU
Number of Residues4
DetailsCOPPER COORDINATION SITE; ALSO THE ENZYME CATALYTIC SITE.
ChainResidue
ACU1154
AHIS46
AHIS48
AHIS120

site_idZN
Number of Residues5
DetailsZINC COORDINATION SITE.
ChainResidue
AHIS63
AHIS71
AHIS80
AASP83
AZN155

Functional Information from PROSITE/UniProt
site_idPS00087
Number of Residues11
DetailsSOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. GFHIHEfGDaT
ChainResidueDetails
AGLY44-THR54

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: in apo form => ECO:0000269|PubMed:10026301, ECO:0000269|PubMed:11524675
ChainResidueDetails
AARG43

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:10026301, ECO:0000269|PubMed:8652572
ChainResidueDetails
AILE47
AGLU49
AALA121

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10026301, ECO:0000269|PubMed:11524675
ChainResidueDetails
APHE64
AGLY72
AVAL81
AMET84

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
APRO144

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
AGLU26

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
APRO39

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
APHE99

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358
ChainResidueDetails
AVAL117

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17287358
ChainResidueDetails
AGLU132

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198
ChainResidueDetails
AGLY138

site_idSWS_FT_FI11
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:15166219
ChainResidueDetails
APHE19
ATHR70

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
AILE47metal ligand
AGLU49metal ligand
APHE64hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
AGLY72metal ligand
AVAL81metal ligand
AMET84metal ligand
AALA121metal ligand
APRO144electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-07-17

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