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4BXH

Resolving the activation site of positive regulators in plant phosphoenolpyruvate carboxylase

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 Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1002
ChainResidue
AARG450
AARG767
AALA768
AILE769
AHOH2378
AHOH2379

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1003
ChainResidue
AASN964
ATHR965
AGLY966
AHOH2323
AGLY636
AGLY637
AGLN667

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1004
ChainResidue
AARG178
AARG179
ASER180
AARG366

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 1002
ChainResidue
BARG450
BARG767
BALA768
BILE769
BHOH2296
BHOH2366

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 1003
ChainResidue
BGLY636
BGLY637
BARG641
BGLN667
BASN964
BTHR965
BGLY966

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1004
ChainResidue
BARG178
BARG179
BSER180
BARG366

Functional Information from PROSITE/UniProt
site_idPS00393
Number of Residues13
DetailsPEPCASE_2 Phosphoenolpyruvate carboxylase active site 2. VMIGYSDSgKDAG
ChainResidueDetails
BVAL591-GLY603
AVAL591-GLY603

site_idPS00781
Number of Residues12
DetailsPEPCASE_1 Phosphoenolpyruvate carboxylase active site 1. VlTAHPTQsvRR
ChainResidueDetails
BVAL168-ARG179
AVAL168-ARG179

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P04711
ChainResidueDetails
BHIS172
BLYS600
BARG641

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:24043710, ECO:0007744|PDB:4BXC
ChainResidueDetails
BTRP283
BARG450
BASP597
BARG635
BTHR665
BARG753
BARG767

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:23443546, ECO:0007744|PDB:3ZGE
ChainResidueDetails
BARG641
BGLN673
BLYS829
BARG888
BASN964

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04711
ChainResidueDetails
BSER11

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PDB entries from 2024-07-10

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