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2DE5

Crystal structure of the electron transfer complex between oxygenase and ferredoxin in carbazole 1,9a-dioxygenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0046872molecular_functionmetal ion binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0046872molecular_functionmetal ion binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
C0046872molecular_functionmetal ion binding
C0051537molecular_function2 iron, 2 sulfur cluster binding
D0008901molecular_functionferredoxin hydrogenase activity
D0046232biological_processcarbazole catabolic process
D0046872molecular_functionmetal ion binding
D0051213molecular_functiondioxygenase activity
D0051537molecular_function2 iron, 2 sulfur cluster binding
E0008901molecular_functionferredoxin hydrogenase activity
E0046232biological_processcarbazole catabolic process
E0046872molecular_functionmetal ion binding
E0051213molecular_functiondioxygenase activity
E0051537molecular_function2 iron, 2 sulfur cluster binding
F0008901molecular_functionferredoxin hydrogenase activity
F0046232biological_processcarbazole catabolic process
F0046872molecular_functionmetal ion binding
F0051213molecular_functiondioxygenase activity
F0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 A 501
ChainResidue
AHIS183
AHIS187
AASP333
AHOH635

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 B 501
ChainResidue
BHIS183
BHIS187
BASP333
BHOH746

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 C 501
ChainResidue
CHIS187
CASP333
CHOH707
CHIS183

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES A 401
ChainResidue
ACYS69
AHIS71
AARG72
AVAL74
ACYS90
ATYR92
AHIS93
ATRP95

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES B 401
ChainResidue
BCYS69
BHIS71
BARG72
BCYS90
BTYR92
BHIS93
BTRP95

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES C 401
ChainResidue
CCYS69
CHIS71
CARG72
CCYS90
CTYR92
CHIS93
CTRP95

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES D 201
ChainResidue
DCYS46
DHIS48
DGLY49
DCYS65
DHIS68
DGLY70

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES E 201
ChainResidue
ECYS46
EHIS48
EGLY49
ECYS65
EHIS68
EGLY70

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES F 201
ChainResidue
FCYS46
FHIS48
FGLY49
FCYS65
FHIS68
FGLY70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:15645447, ECO:0000269|PubMed:17161368
ChainResidueDetails
DCYS46
FHIS48
FCYS65
FHIS68
DHIS48
DCYS65
DHIS68
ECYS46
EHIS48
ECYS65
EHIS68
FCYS46

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ndo
ChainResidueDetails
AASP180
AHIS183
BHIS93

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ndo
ChainResidueDetails
CHIS93
BASP180
BHIS183

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ndo
ChainResidueDetails
AHIS93
CHIS183
CASP180

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PDB entries from 2024-07-24

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