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4HHH

Structure of Pisum sativum Rubisco

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004497molecular_functionmonooxygenase activity
A0009507cellular_componentchloroplast
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
B0000287molecular_functionmagnesium ion binding
B0004497molecular_functionmonooxygenase activity
B0009507cellular_componentchloroplast
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
C0000287molecular_functionmagnesium ion binding
C0004497molecular_functionmonooxygenase activity
C0009507cellular_componentchloroplast
C0009853biological_processphotorespiration
C0015977biological_processcarbon fixation
C0015979biological_processphotosynthesis
C0016491molecular_functionoxidoreductase activity
C0016829molecular_functionlyase activity
C0016984molecular_functionribulose-bisphosphate carboxylase activity
C0019253biological_processreductive pentose-phosphate cycle
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0004497molecular_functionmonooxygenase activity
D0009507cellular_componentchloroplast
D0009853biological_processphotorespiration
D0015977biological_processcarbon fixation
D0015979biological_processphotosynthesis
D0016491molecular_functionoxidoreductase activity
D0016829molecular_functionlyase activity
D0016984molecular_functionribulose-bisphosphate carboxylase activity
D0019253biological_processreductive pentose-phosphate cycle
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE RUB A 501
ChainResidue
ATHR173
ASER379
AGLY380
AGLY381
AGLY403
AGLY404
AHOH622
AHOH634
AHOH661
AHOH662
AHOH682
ALYS177
BTHR65
BTRP66
BASN123
BHOH716
AASP203
AGLU204
AHIS294
AARG295
AHIS327
ALYS334
ALEU335

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE RUB B 501
ChainResidue
ATHR65
ATRP66
AASN123
BLYS175
BASP203
BGLU204
BHIS294
BARG295
BHIS327
BLYS334
BLEU335
BSER379
BGLY380
BGLY381
BGLY403
BGLY404
BHOH611
BHOH638
BHOH682
BHOH684
BHOH691
BHOH728

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE RUB C 501
ChainResidue
CTHR173
CLYS175
CASP203
CGLU204
CHIS294
CARG295
CHIS327
CLEU335
CSER379
CGLY380
CGLY381
CGLY403
CGLY404
CHOH614
CHOH651
CHOH652
CHOH675
CHOH703
CHOH737
DTHR65
DTRP66
DASN123

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE RUB D 501
ChainResidue
CTHR65
CTRP66
CASN123
DLYS175
DLYS177
DASP203
DGLU204
DARG295
DHIS327
DLYS334
DLEU335
DSER379
DGLY381
DGLY403
DGLY404
DHOH709
DHOH717
DHOH719
DHOH720
DHOH745

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 Residues8
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26197050","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MKV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"description":"via carbamate group","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"PubMed","id":"16668742","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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