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3ZGE

Greater efficiency of photosynthetic carbon fixation due to single amino acid substitution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006099biological_processtricarboxylic acid cycle
A0008964molecular_functionphosphoenolpyruvate carboxylase activity
A0009507cellular_componentchloroplast
A0009760biological_processC4 photosynthesis
A0015977biological_processcarbon fixation
A0015979biological_processphotosynthesis
A0016829molecular_functionlyase activity
A0048046cellular_componentapoplast
A0048366biological_processleaf development
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006099biological_processtricarboxylic acid cycle
B0008964molecular_functionphosphoenolpyruvate carboxylase activity
B0009507cellular_componentchloroplast
B0009760biological_processC4 photosynthesis
B0015977biological_processcarbon fixation
B0015979biological_processphotosynthesis
B0016829molecular_functionlyase activity
B0048046cellular_componentapoplast
B0048366biological_processleaf development
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ASP A 1967
ChainResidue
AARG641
AHOH2078
AHOH2116
AGLN673
AMET825
ALYS829
ALEU881
AARG888
AGLN963
AASN964
AHOH2010

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1968
ChainResidue
AARG178
AARG179
ASER180
AARG366

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1969
ChainResidue
AGLY636
AGLY637
AGLN667
AASN964
ATHR965
AGLY966

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ASP B 1967
ChainResidue
BARG641
BGLN673
BMET825
BLYS829
BLEU881
BARG888
BGLN963
BASN964
BHOH2006
BHOH2059
BHOH2082

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1968
ChainResidue
BARG178
BARG179
BSER180
BARG366

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 1969
ChainResidue
BGLY636
BGLY637
BGLN667
BASN964
BTHR965
BGLY966

Functional Information from PROSITE/UniProt
site_idPS00393
Number of Residues13
DetailsPEPCASE_2 Phosphoenolpyruvate carboxylase active site 2. VMIGYSDSgKDAG
ChainResidueDetails
AVAL591-GLY603

site_idPS00781
Number of Residues12
DetailsPEPCASE_1 Phosphoenolpyruvate carboxylase active site 1. VlTAHPTQsvRR
ChainResidueDetails
AVAL168-ARG179

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P04711
ChainResidueDetails
AHIS172
ALYS600
AARG641
BHIS172
BLYS600
BARG641

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:24043710, ECO:0007744|PDB:4BXC
ChainResidueDetails
ATRP283
BASP597
BARG635
BTHR665
BARG753
BARG767
AARG450
AASP597
AARG635
ATHR665
AARG753
AARG767
BTRP283
BARG450

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:23443546, ECO:0007744|PDB:3ZGE
ChainResidueDetails
AARG641
BASN964
AGLN673
ALYS829
AARG888
AASN964
BARG641
BGLN673
BLYS829
BARG888

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04711
ChainResidueDetails
ASER11
BSER11

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PDB entries from 2024-07-10

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