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1DO6

CRYSTAL STRUCTURE OF SUPEROXIDE REDUCTASE IN THE OXIDIZED STATE AT 2.0 ANGSTROM RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0050605molecular_functionsuperoxide reductase activity
A0098869biological_processcellular oxidant detoxification
B0005506molecular_functioniron ion binding
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0050605molecular_functionsuperoxide reductase activity
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 200
ChainResidue
AGLU14
AHIS16
AHIS41
AHIS47
ACYS111
AHIS114

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE B 205
ChainResidue
BHIS47
BCYS111
BHIS114
BLYS15
BHIS16
BHIS41

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AGLU14
BHIS47
BCYS111
BHIS114
AHIS16
AHIS41
AHIS47
ACYS111
AHIS114
BGLU14
BHIS16
BHIS41

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 10704199, 11914081, 11489883
ChainResidueDetails
ALYS15
AGLU14

site_idCSA2
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 10704199, 11914081, 11489883
ChainResidueDetails
BLYS15
BGLU14

site_idMCSA1
Number of Residues7
DetailsM-CSA 660
ChainResidueDetails
AGLU14electrostatic stabiliser, metal ligand, nucleophile
ALYS15proton donor
AHIS16metal ligand
AHIS41metal ligand
AHIS47metal ligand
ACYS111metal ligand
AHIS114metal ligand

site_idMCSA2
Number of Residues7
DetailsM-CSA 660
ChainResidueDetails
BGLU14electrostatic stabiliser, metal ligand, nucleophile
BLYS15proton donor
BHIS16metal ligand
BHIS41metal ligand
BHIS47metal ligand
BCYS111metal ligand
BHIS114metal ligand

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PDB entries from 2024-07-17

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