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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 Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P04179
ChainResidueDetails
AHIS26
CHIS81
CASP168
CHIS172
DHIS26
DHIS81
DASP168
DHIS172
AHIS81
AASP168
AHIS172
BHIS26
BHIS81
BASP168
BHIS172
CHIS26

site_idSWS_FT_FI2
Number of Residues8
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17761666
ChainResidueDetails
ATHR121
ATHR123
BTHR121
BTHR123
CTHR121
CTHR123
DTHR121
DTHR123

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PDB entries from 2024-07-17

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