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1IDS

X-RAY STRUCTURE ANALYSIS OF THE IRON-DEPENDENT SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS AT 2.0 ANGSTROMS RESOLUTIONS REVEALS NOVEL DIMER-DIMER INTERACTIONS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004784molecular_functionsuperoxide dismutase activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006801biological_processsuperoxide metabolic process
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0098754biological_processdetoxification
B0004784molecular_functionsuperoxide dismutase activity
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006801biological_processsuperoxide metabolic process
B0006979biological_processresponse to oxidative stress
B0016491molecular_functionoxidoreductase activity
B0019430biological_processremoval of superoxide radicals
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
B0098754biological_processdetoxification
C0004784molecular_functionsuperoxide dismutase activity
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006801biological_processsuperoxide metabolic process
C0006979biological_processresponse to oxidative stress
C0016491molecular_functionoxidoreductase activity
C0019430biological_processremoval of superoxide radicals
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
C0098754biological_processdetoxification
D0004784molecular_functionsuperoxide dismutase activity
D0005506molecular_functioniron ion binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006801biological_processsuperoxide metabolic process
D0006979biological_processresponse to oxidative stress
D0016491molecular_functionoxidoreductase activity
D0019430biological_processremoval of superoxide radicals
D0042597cellular_componentperiplasmic space
D0046872molecular_functionmetal ion binding
D0098754biological_processdetoxification
Functional Information from PDB Data
site_idA1
Number of Residues1
DetailsCATALYTIC SITE OF CHAIN A
ChainResidue
AFE208

site_idA2
Number of Residues1
DetailsCATALYTIC SITE OF CHAIN B
ChainResidue
BFE208

site_idA3
Number of Residues1
DetailsCATALYTIC SITE OF CHAIN C
ChainResidue
CFE208

site_idA4
Number of Residues1
DetailsCATALYTIC SITE OF CHAIN D
ChainResidue
DFE208

site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 208
ChainResidue
AHIS28
AHIS76
AASP160
AHIS164
AHOH1001

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B 208
ChainResidue
BHIS28
BHIS76
BASP160
BHIS164
BHOH1002

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE C 208
ChainResidue
CHIS28
CHIS76
CASP160
CHIS164
CHOH1003

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE D 208
ChainResidue
DHIS28
DHIS76
DASP160
DHIS164
DHOH1004

Functional Information from PROSITE/UniProt
site_idPS00088
Number of Residues8
DetailsSOD_MN Manganese and iron superoxide dismutases signature. DmWEHAFY
ChainResidueDetails
AASP160-TYR167

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:11747311, ECO:0000269|PubMed:7877174, ECO:0000269|PubMed:8674528, ECO:0000269|PubMed:9490054, ECO:0007744|PDB:1GN2, ECO:0007744|PDB:1GN3, ECO:0007744|PDB:1GN6, ECO:0007744|PDB:1IDS
ChainResidueDetails
AHIS28
CHIS76
CASP160
CHIS164
DHIS28
DHIS76
DASP160
DHIS164
AHIS76
AASP160
AHIS164
BHIS28
BHIS76
BASP160
BHIS164
CHIS28

site_idSWS_FT_FI2
Number of Residues8
DetailsCROSSLNK: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) => ECO:0000269|PubMed:20066036
ChainResidueDetails
ALYS202
BLYS202
CLYS202
DLYS202

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PDB entries from 2024-10-02

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