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3LB8

Crystal structure of the covalent putidaredoxin reductase-putidaredoxin complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
A0019383biological_process(+)-camphor catabolic process
A0050660molecular_functionflavin adenine dinucleotide binding
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
B0019383biological_process(+)-camphor catabolic process
B0050660molecular_functionflavin adenine dinucleotide binding
C0005515molecular_functionprotein binding
C0005829cellular_componentcytosol
C0046872molecular_functionmetal ion binding
C0051536molecular_functioniron-sulfur cluster binding
C0051537molecular_function2 iron, 2 sulfur cluster binding
C0140647biological_processP450-containing electron transport chain
D0005515molecular_functionprotein binding
D0005829cellular_componentcytosol
D0046872molecular_functionmetal ion binding
D0051536molecular_functioniron-sulfur cluster binding
D0051537molecular_function2 iron, 2 sulfur cluster binding
D0140647biological_processP450-containing electron transport chain
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR RESIDUE FAD A 449
ChainResidue
AHOH1
ASER49
ALYS50
ATHR81
AGLN82
AVAL83
AALA109
ATHR110
AGLY111
AGLY112
AARG134
AGLY11
AILE160
AASP284
AGLU300
ASER301
AVAL302
APRO303
APHE329
ATRP330
AHOH438
AHOH439
AGLY13
AHOH471
AHOH475
ALEU14
AALA15
AGLY36
AASP37
ALEU45
APRO46

site_idAC2
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD B 449
ChainResidue
BVAL10
BGLY11
BGLY13
BLEU14
BALA15
BGLY36
BASP37
BLEU45
BPRO46
BSER49
BLYS50
BTHR81
BVAL83
BALA109
BTHR110
BGLY111
BGLY112
BLEU133
BARG134
BILE160
BASN251
BLEU254
BGLY283
BASP284
BGLU300
BSER301
BVAL302
BPRO303
BPHE329
BTRP330
BHOH438
BHOH443

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FES C 107
ChainResidue
CGLY37
CCYS39
CGLY41
CALA43
CSER44
CCYS45
CALA46
CCYS48
CCYS86

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FES D 107
ChainResidue
DGLY37
DCYS39
DGLY40
DGLY41
DALA43
DSER44
DCYS45
DCYS48
DLEU84
DCYS86

Functional Information from PROSITE/UniProt
site_idPS00814
Number of Residues11
DetailsADX Adrenodoxin family, iron-sulfur binding region signature. CggSaSCATCH
ChainResidueDetails
CCYS39-HIS49

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00465, ECO:0000269|PubMed:8204575
ChainResidueDetails
CCYS39
CCYS45
CCYS48
CCYS86
DCYS39
DCYS45
DCYS48
DCYS86

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15095867, ECO:0000269|PubMed:20179327, ECO:0007744|PDB:1Q1R, ECO:0007744|PDB:3LB8
ChainResidueDetails
AARG134
AASP284
AVAL302
BARG134
BASP284
BVAL302

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY156
BGLY156

225946

PDB entries from 2024-10-09

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