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3LSU

Crystal Structure of SOD2 from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004784molecular_functionsuperoxide dismutase activity
A0006801biological_processsuperoxide metabolic process
A0046872molecular_functionmetal ion binding
B0004784molecular_functionsuperoxide dismutase activity
B0006801biological_processsuperoxide metabolic process
B0046872molecular_functionmetal ion binding
C0004784molecular_functionsuperoxide dismutase activity
C0006801biological_processsuperoxide metabolic process
C0046872molecular_functionmetal ion binding
D0004784molecular_functionsuperoxide dismutase activity
D0006801biological_processsuperoxide metabolic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 208
ChainResidue
AHIS26
AHIS81
AASP168
AHIS172
AHOH211

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 208
ChainResidue
BHOH214
BHIS26
BHIS81
BASP168
BHIS172

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 209
ChainResidue
AMLY8
AGLN93
AASN194
BHOH230

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN C 208
ChainResidue
CHIS26
CHIS81
CASP168
CHIS172
CHOH212

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA C 209
ChainResidue
CGLN177
CGLN179
CGOL210
CHOH222
CHOH259

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL C 210
ChainResidue
AGLY12
AGLU15
CGLN177
CTYR178
CMLY181
CASP184
CNA209
CHOH259

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN D 208
ChainResidue
DHIS26
DHIS81
DASP168
DHIS172
DHOH214

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 209
ChainResidue
BGLU15
BGLY20
BGLN21
DTYR178
DMLY181
DASP184
DHOH257

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL D 210
ChainResidue
BGLU15
BPRO16
BILE18
BSER19
BGLN177
DPRO16

Functional Information from PROSITE/UniProt
site_idPS00088
Number of Residues8
DetailsSOD_MN Manganese and iron superoxide dismutases signature. DaWEHAYY
ChainResidueDetails
AASP168-TYR175

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04179","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17761666","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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