Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2BKB

q69e-FeSOD

Functional Information from GO Data
ChainGOidnamespacecontents
A0000303biological_processresponse to superoxide
A0004784molecular_functionsuperoxide dismutase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006801biological_processsuperoxide metabolic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0046872molecular_functionmetal ion binding
B0000303biological_processresponse to superoxide
B0004784molecular_functionsuperoxide dismutase activity
B0005506molecular_functioniron ion binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006801biological_processsuperoxide metabolic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0019430biological_processremoval of superoxide radicals
B0046872molecular_functionmetal ion binding
C0000303biological_processresponse to superoxide
C0004784molecular_functionsuperoxide dismutase activity
C0005506molecular_functioniron ion binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006801biological_processsuperoxide metabolic process
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0019430biological_processremoval of superoxide radicals
C0046872molecular_functionmetal ion binding
D0000303biological_processresponse to superoxide
D0004784molecular_functionsuperoxide dismutase activity
D0005506molecular_functioniron ion binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006801biological_processsuperoxide metabolic process
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0019430biological_processremoval of superoxide radicals
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A1193
ChainResidue
AHIS26
AHIS73
AASP156
AHIS160
AHOH2081

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 B1393
ChainResidue
BHOH2078
BHIS226
BHIS273
BASP356
BHIS360

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 C1193
ChainResidue
CHIS26
CHIS73
CASP156
CHIS160
CHOH2052

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 D1393
ChainResidue
DHIS226
DHIS273
DASP356
DHIS360
DHOH2058

Functional Information from PROSITE/UniProt
site_idPS00088
Number of Residues8
DetailsSOD_MN Manganese and iron superoxide dismutases signature. DvWEHAYY
ChainResidueDetails
AASP156-TYR163

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING:
ChainResidueDetails
ATYR27
CTHR74
CVAL157
CALA161
DTYR227
DTHR274
DVAL357
DALA361
ATHR74
AVAL157
AALA161
BTYR227
BTHR274
BVAL357
BALA361
CTYR27

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ASER51
BSER251
CSER51
DSER251

226262

PDB entries from 2024-10-16

PDB statisticsPDBj update infoContact PDBjnumon