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1GAQ

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN FERREDOXIN AND FERREDOXIN-NADP+ REDUCTASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
B0009055molecular_functionelectron transfer activity
B0022900biological_processelectron transport chain
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
C0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FAD A 320
ChainResidue
AARG93
AGLY130
AVAL131
ACYS132
ASER133
ATHR172
ATYR314
AHOH334
AHOH351
BSER38
BGLU94
ALEU94
CTHR121
CFAD321
ATYR95
ASER96
ACYS114
AVAL115
ALYS116
ALEU118
ATYR120

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES B 99
ChainResidue
BSER38
BCYS39
BARG40
BGLY42
BSER43
BCYS44
BCYS47
BCYS77

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FAD C 321
ChainResidue
AFAD320
CARG93
CLEU94
CTYR95
CSER96
CCYS114
CLYS116
CLEU118
CTYR120
CGLY130
CVAL131
CCYS132
CSER133
CTHR172
CGLU312
CTYR314
CHOH348
CHOH351

Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CRAGSCSSC
ChainResidueDetails
BCYS39-CYS47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BCYS39
BCYS44
BCYS47
BCYS77

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
ACYS272
ASER96
AGLU312

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
CCYS272
CSER96
CGLU312

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
ATYR95

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
CTYR95

229183

PDB entries from 2024-12-18

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