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3AXK

Structure of rice Rubisco in complex with NADP(H)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004497molecular_functionmonooxygenase activity
A0009507cellular_componentchloroplast
A0009536cellular_componentplastid
A0009853biological_processphotorespiration
A0015977biological_processcarbon fixation
A0015979biological_processphotosynthesis
A0016491molecular_functionoxidoreductase activity
A0016829molecular_functionlyase activity
A0016984molecular_functionribulose-bisphosphate carboxylase activity
A0019253biological_processreductive pentose-phosphate cycle
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004497molecular_functionmonooxygenase activity
B0009507cellular_componentchloroplast
B0009536cellular_componentplastid
B0009853biological_processphotorespiration
B0015977biological_processcarbon fixation
B0015979biological_processphotosynthesis
B0016491molecular_functionoxidoreductase activity
B0016829molecular_functionlyase activity
B0016984molecular_functionribulose-bisphosphate carboxylase activity
B0019253biological_processreductive pentose-phosphate cycle
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
ALEU270
AGLY273
AMET297
AILE301
AHOH627
AHOH628
AHOH629
BLEU270
BILE301

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
AHIS86
AGLU88
ALYS356
AARG358
BHOH976

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 478
ChainResidue
AKCX201
AASP203
AGLU204
AHOH616
AHOH693
AHOH901

site_idAC4
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NDP A 479
ChainResidue
ALYS175
AHIS294
AARG295
AHIS298
ASER379
AGLY380
AGLY381
AGLY403
AGLY404
AGLY405
AHOH580
AHOH595
AHOH614
AHOH616
AHOH693
AHOH758
AHOH1073
AHOH1080
AHOH1081
AHOH1083
AHOH1085
AHOH1086
AHOH1115
BGLU60
BASN123
BGLY126
BPHE127
BHOH733

site_idAC5
Number of Residues32
DetailsBINDING SITE FOR RESIDUE NDP A 480
ChainResidue
AGLU60
ATHR68
AASN123
AGLY126
APHE127
AHOH534
AHOH594
AHOH854
AHOH1074
AHOH1076
AHOH1090
AHOH1091
AHOH1092
AHOH1093
AHOH1096
BLYS175
BHIS294
BARG295
BHIS298
BSER379
BGLY380
BGLY381
BILE382
BGLY404
BGLY405
BHOH696
BHOH787
BHOH855
BHOH1078
BHOH1079
BHOH1087
BHOH1125

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 503
ChainResidue
ASER145
ALYS146
APHE148
AARG213
AHOH497
AHOH539
AHOH1109
BGLU110
BGOL504

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 504
ChainResidue
ALYS146
ATHR147
AHOH894
AHOH895
BGOL503
BHOH654

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 478
ChainResidue
BHOH787
BHOH855
BKCX201
BASP203
BGLU204
BHOH734

Functional Information from PROSITE/UniProt
site_idPS00157
Number of Residues9
DetailsRUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFtKdDE
ChainResidueDetails
AGLY196-GLU204

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01338
ChainResidueDetails
ALYS175
AHIS294
BLYS175
BHIS294

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:22609438, ECO:0007744|PDB:3AXK
ChainResidueDetails
AGLU60
BLYS175
BARG295
BGLY381
ATHR68
APHE127
ALYS175
AARG295
AGLY381
BGLU60
BTHR68
BPHE127

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:22609438, ECO:0007744|PDB:1WDD
ChainResidueDetails
ATHR65
ATHR173
AHIS327
ASER379
BTHR65
BTHR173
BHIS327
BSER379

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: in homodimeric partner => ECO:0000269|PubMed:22609438, ECO:0007744|PDB:1WDD, ECO:0007744|PDB:3AXM
ChainResidueDetails
AASN123
BASN123

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: via carbamate group => ECO:0000269|PubMed:22609438, ECO:0007744|PDB:1WDD, ECO:0007744|PDB:3AXK, ECO:0007744|PDB:3AXM
ChainResidueDetails
AKCX201
BKCX201

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22609438, ECO:0007744|PDB:1WDD, ECO:0007744|PDB:3AXK, ECO:0007744|PDB:3AXM
ChainResidueDetails
AASP203
AGLU204
BASP203
BGLU204

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:1WDD
ChainResidueDetails
AHIS294
ALYS334
BHIS294
BLYS334

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22609438
ChainResidueDetails
AGLY404
BGLY404

site_idSWS_FT_FI9
Number of Residues2
DetailsSITE: Transition state stabilizer
ChainResidueDetails
ALYS334
BLYS334

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N-acetylproline => ECO:0000250
ChainResidueDetails
APRO3
BPRO3

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-carboxylysine => ECO:0000269|PubMed:22609438
ChainResidueDetails
AKCX201
BKCX201

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PDB entries from 2025-06-18

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