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5NCC

Structure of Fatty acid Photodecarboxylase in complex with FAD and palmitic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0009507cellular_componentchloroplast
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0016829molecular_functionlyase activity
A0050660molecular_functionflavin adenine dinucleotide binding
B0009507cellular_componentchloroplast
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0016829molecular_functionlyase activity
B0050660molecular_functionflavin adenine dinucleotide binding
C0009507cellular_componentchloroplast
C0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
C0016829molecular_functionlyase activity
C0050660molecular_functionflavin adenine dinucleotide binding
D0009507cellular_componentchloroplast
D0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
D0016829molecular_functionlyase activity
D0050660molecular_functionflavin adenine dinucleotide binding
E0009507cellular_componentchloroplast
E0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
E0016829molecular_functionlyase activity
E0050660molecular_functionflavin adenine dinucleotide binding
F0009507cellular_componentchloroplast
F0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
F0016829molecular_functionlyase activity
F0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues36
Detailsbinding site for residue FAD A 701
ChainResidue
AGLY90
AALA158
AARG159
AGLY160
AARG161
ALEU162
AGLY165
ASER166
ASER167
AASN170
AALA171
AGLY92
ATHR172
ALEU173
AALA296
AVAL298
ACYS340
AALA341
AGLY342
AHIS345
ALEU349
AASN575
ATHR93
AASP609
AALA610
AGLN620
ATHR621
AGLY622
AVAL625
APLM702
AALA94
ALEU113
AGLU114
AALA115
APHE134
ATRP140

site_idAC2
Number of Residues12
Detailsbinding site for residue PLM A 702
ChainResidue
AALA171
AARG451
AVAL453
AALA457
AGLY462
ATHR465
ATYR466
APHE469
ATHR484
AGLN486
AASN575
AFAD701

site_idAC3
Number of Residues36
Detailsbinding site for residue FAD B 701
ChainResidue
BGLY90
BGLY92
BTHR93
BALA94
BLEU113
BGLU114
BALA115
BPHE134
BTRP140
BALA158
BARG159
BGLY160
BARG161
BLEU162
BGLY165
BSER166
BSER167
BASN170
BALA171
BTHR172
BLEU173
BALA296
BVAL298
BCYS340
BALA341
BGLY342
BHIS345
BLEU349
BASN575
BASP609
BALA610
BGLN620
BTHR621
BGLY622
BVAL625
BPLM702

site_idAC4
Number of Residues10
Detailsbinding site for residue PLM B 702
ChainResidue
BALA171
BARG451
BVAL453
BMET456
BALA457
BTHR465
BTYR466
BGLN486
BASN575
BFAD701

site_idAC5
Number of Residues34
Detailsbinding site for residue FAD C 701
ChainResidue
CGLU114
CALA115
CPHE134
CTRP140
CALA158
CARG159
CGLY160
CLEU162
CGLY165
CSER166
CSER167
CASN170
CALA171
CTHR172
CLEU173
CALA296
CALA297
CVAL298
CCYS340
CALA341
CGLY342
CHIS345
CASN575
CASP609
CALA610
CGLN620
CTHR621
CGLY622
CVAL625
CGLY90
CGLY92
CTHR93
CALA94
CLEU113

site_idAC6
Number of Residues11
Detailsbinding site for residue PLM C 702
ChainResidue
CALA171
CARG451
CVAL453
CMET456
CALA457
CGLY462
CTHR465
CTYR466
CGLN486
CSER574
CASN575

site_idAC7
Number of Residues35
Detailsbinding site for residue FAD D 701
ChainResidue
DGLY90
DGLY92
DTHR93
DALA94
DLEU113
DGLU114
DALA115
DPHE134
DTRP140
DALA158
DARG159
DGLY160
DLEU162
DGLY165
DSER166
DSER167
DASN170
DALA171
DTHR172
DLEU173
DALA296
DALA297
DVAL298
DCYS340
DALA341
DGLY342
DHIS345
DLEU349
DASN575
DASP609
DALA610
DGLN620
DTHR621
DGLY622
DVAL625

site_idAC8
Number of Residues9
Detailsbinding site for residue PLM D 702
ChainResidue
DARG451
DVAL453
DGLY462
DTHR465
DTYR466
DTHR484
DGLN486
DSER574
DASN575

site_idAC9
Number of Residues31
Detailsbinding site for residue FAD E 701
ChainResidue
EGLY90
ETHR93
ELEU113
EGLU114
EALA115
EPHE134
ETRP140
EALA158
EARG159
EGLY160
ELEU162
EGLY165
ESER166
ESER167
EASN170
EALA171
ETHR172
ELEU173
EALA296
EALA297
EVAL298
EALA341
EGLY342
EHIS345
EASN575
EASP609
EALA610
EGLN620
ETHR621
EGLY622
EVAL625

site_idAD1
Number of Residues32
Detailsbinding site for residue FAD F 701
ChainResidue
FGLY90
FGLY92
FTHR93
FALA94
FLEU113
FGLU114
FPHE134
FTRP140
FALA158
FGLY160
FARG161
FLEU162
FGLY165
FSER166
FTHR169
FASN170
FALA171
FTHR172
FLEU173
FVAL298
FCYS340
FALA341
FGLY342
FHIS345
FLEU349
FASN575
FASP609
FALA610
FGLN620
FTHR621
FGLY622
FVAL625

Functional Information from PROSITE/UniProt
site_idPS00624
Number of Residues15
DetailsGMC_OXRED_2 GMC oxidoreductases signature 2. GAvhTPfLLkhSGVG
ChainResidueDetails
AGLY342-GLY356

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues66
DetailsBINDING: BINDING => ECO:0000269|PubMed:28860382, ECO:0007744|PDB:5NCC
ChainResidueDetails
ATHR93
AGLN486
AGLY622
BTHR93
BGLU114
BLEU162
BSER166
BASN170
BVAL298
BCYS432
BARG451
AGLU114
BTYR466
BGLN486
BGLY622
CTHR93
CGLU114
CLEU162
CSER166
CASN170
CVAL298
CCYS432
ALEU162
CARG451
CTYR466
CGLN486
CGLY622
DTHR93
DGLU114
DLEU162
DSER166
DASN170
DVAL298
ASER166
DCYS432
DARG451
DTYR466
DGLN486
DGLY622
ETHR93
EGLU114
ELEU162
ESER166
EASN170
AASN170
EVAL298
ECYS432
EARG451
ETYR466
EGLN486
EGLY622
FTHR93
FGLU114
FLEU162
FSER166
AVAL298
FASN170
FVAL298
FCYS432
FARG451
FTYR466
FGLN486
FGLY622
ACYS432
AARG451
ATYR466

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PDB entries from 2024-07-17

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