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2VNK

X-RAY STRUCTURE OF THE FERREDOXIN-NADP(H) REDUCTASE FROM RHODOBACTER CAPSULATUS IN COMPLEX WITH NADP. FORM III AT 1.93 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004324molecular_functionferredoxin-NADP+ reductase activity
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0034599biological_processcellular response to oxidative stress
A0042167biological_processheme catabolic process
B0000166molecular_functionnucleotide binding
B0004324molecular_functionferredoxin-NADP+ reductase activity
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0034599biological_processcellular response to oxidative stress
B0042167biological_processheme catabolic process
C0000166molecular_functionnucleotide binding
C0004324molecular_functionferredoxin-NADP+ reductase activity
C0005737cellular_componentcytoplasm
C0016491molecular_functionoxidoreductase activity
C0034599biological_processcellular response to oxidative stress
C0042167biological_processheme catabolic process
D0000166molecular_functionnucleotide binding
D0004324molecular_functionferredoxin-NADP+ reductase activity
D0005737cellular_componentcytoplasm
D0016491molecular_functionoxidoreductase activity
D0034599biological_processcellular response to oxidative stress
D0042167biological_processheme catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues30
DetailsBINDING SITE FOR RESIDUE FAD A 273
ChainResidue
AARG64
APRO88
ALEU89
ATHR90
ATHR130
AALA133
ALYS265
AALA266
APHE267
AVAL268
AGLU270
AALA65
AGLY271
AILE272
AHOH2057
AHOH2058
AHOH2205
AHOH2209
AHOH2210
AHOH2211
AHOH2212
AHOH2213
ATYR66
AHOH2214
ASER67
ATYR80
ASER81
AILE82
AVAL84
AGLY87

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE NAP A 274
ChainResidue
ATHR128
ACYS157
AARG158
ATHR194
AARG195
AARG203
ATHR205
AALA236
APHE237
AASP240
AGLU270
AHOH2166
AHOH2215
AHOH2216
AHOH2217
AHOH2218
AHOH2219

site_idAC3
Number of Residues28
DetailsBINDING SITE FOR RESIDUE FAD B 273
ChainResidue
BARG64
BALA65
BTYR66
BSER67
BTYR80
BSER81
BILE82
BVAL84
BGLY87
BPRO88
BLEU89
BTHR90
BTHR130
BALA133
BLYS265
BALA266
BPHE267
BVAL268
BGLY269
BHOH2038
BHOH2039
BHOH2203
BHOH2206
BHOH2207
BHOH2208
BHOH2209
BHOH2210
BHOH2211

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NAP B 274
ChainResidue
BTHR128
BCYS157
BARG158
BTHR194
BARG195
BARG203
BTHR205
BALA236
BPHE237
BASP240
BHOH2104
BHOH2212
BHOH2213
BHOH2214
BHOH2215

site_idAC5
Number of Residues31
DetailsBINDING SITE FOR RESIDUE FAD C 273
ChainResidue
CPRO88
CLEU89
CTHR90
CTHR130
CALA133
CLYS265
CALA266
CPHE267
CVAL268
CGLY269
CGLU270
CGLY271
CILE272
CHOH2060
CHOH2061
CHOH2226
CHOH2227
CHOH2228
CHOH2229
CHOH2230
CHOH2231
CHOH2232
CARG64
CALA65
CTYR66
CSER67
CTYR80
CSER81
CILE82
CVAL84
CGLY87

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE NAP C 274
ChainResidue
CTHR128
CCYS157
CARG158
CTHR194
CARG195
CARG203
CTHR205
CALA236
CPHE237
CASP240
CILE272
CHOH2139
CHOH2175
CHOH2233
CHOH2234
CHOH2235
CHOH2236

site_idAC7
Number of Residues28
DetailsBINDING SITE FOR RESIDUE FAD D 273
ChainResidue
DARG64
DALA65
DTYR66
DSER67
DTYR80
DSER81
DILE82
DVAL84
DGLY87
DPRO88
DLEU89
DTHR90
DTHR130
DALA133
DLYS265
DALA266
DPHE267
DVAL268
DGLY269
DHOH2038
DHOH2040
DHOH2199
DHOH2202
DHOH2203
DHOH2204
DHOH2205
DHOH2206
DHOH2207

site_idAC8
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NAP D 274
ChainResidue
DTHR128
DCYS157
DARG158
DTHR194
DARG195
DARG203
DTHR205
DALA236
DPHE237
DASP240
DHOH2101
DHOH2208
DHOH2209
DHOH2210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16128574","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18973834","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24016470","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18973834","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16128574","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18973834","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ndh
ChainResidueDetails
ATYR66

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ndh
ChainResidueDetails
BTYR66

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ndh
ChainResidueDetails
CTYR66

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ndh
ChainResidueDetails
DTYR66

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PDB entries from 2025-12-24

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