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2AQT

CU/ZN superoxide dismutase from neisseria meningitidis K91Q, K94Q double mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004784molecular_functionsuperoxide dismutase activity
A0005507molecular_functioncopper ion binding
A0006801biological_processsuperoxide metabolic process
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
B0004784molecular_functionsuperoxide dismutase activity
B0005507molecular_functioncopper ion binding
B0006801biological_processsuperoxide metabolic process
B0016209molecular_functionantioxidant activity
B0016491molecular_functionoxidoreductase activity
B0019430biological_processremoval of superoxide radicals
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
C0004784molecular_functionsuperoxide dismutase activity
C0005507molecular_functioncopper ion binding
C0006801biological_processsuperoxide metabolic process
C0016209molecular_functionantioxidant activity
C0016491molecular_functionoxidoreductase activity
C0019430biological_processremoval of superoxide radicals
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
C0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU1 C 200
ChainResidue
CHIS79
CHIS81
CHIS104
CHIS160

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 201
ChainResidue
CHIS104
CHIS113
CHIS122
CASP125

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU1 B 200
ChainResidue
BHIS81
BHIS104
BHIS160
BHIS79

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 201
ChainResidue
BHIS104
BHIS113
BHIS122
BASP125

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU1 A 200
ChainResidue
AHIS79
AHIS81
AHIS104
AHIS160

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 201
ChainResidue
AHIS104
AHIS113
AHIS122
AASP125

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 300
ChainResidue
AGLU73
AHIS133
BGLU73
BHIS133

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 301
ChainResidue
CGLU73
CGLU73
CHIS133
CHIS133

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 800
ChainResidue
AASN59
ALYS111
BGLN118
BASP119
BASP120
BHOH489

Functional Information from PROSITE/UniProt
site_idPS00087
Number of Residues11
DetailsSOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. GFHIHEnPScE
ChainResidueDetails
CGLY77-GLU87

site_idPS00332
Number of Residues12
DetailsSOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GGGGpRmACgvI
ChainResidueDetails
CGLY174-ILE185

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
CHIS79
BHIS104
BHIS113
BHIS122
BASP125
BHIS160
AHIS79
AHIS81
AHIS104
AHIS113
AHIS122
CHIS81
AASP125
AHIS160
CHIS104
CHIS113
CHIS122
CASP125
CHIS160
BHIS79
BHIS81

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
CARG179
CHIS104

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
BARG179
BHIS104

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
AARG179
AHIS104

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
CHIS104

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
BHIS104

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 2jcw
ChainResidueDetails
AHIS104

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PDB entries from 2024-07-10

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