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5VYJ

Crystal structure of the photosynthetic phosphoenolpyruvate carboxylase isoenzyme from maize in complex with Gly

Replaces:  4UOL
Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006099biological_processtricarboxylic acid cycle
A0008964molecular_functionphosphoenolpyruvate carboxylase activity
A0009735biological_processresponse to cytokinin
A0010167biological_processresponse to nitrate
A0015977biological_processcarbon fixation
A0015979biological_processphotosynthesis
A0016829molecular_functionlyase activity
A0048366biological_processleaf development
A0060359biological_processresponse to ammonium ion
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006099biological_processtricarboxylic acid cycle
B0008964molecular_functionphosphoenolpyruvate carboxylase activity
B0009735biological_processresponse to cytokinin
B0010167biological_processresponse to nitrate
B0015977biological_processcarbon fixation
B0015979biological_processphotosynthesis
B0016829molecular_functionlyase activity
B0048366biological_processleaf development
B0060359biological_processresponse to ammonium ion
C0003824molecular_functioncatalytic activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006099biological_processtricarboxylic acid cycle
C0008964molecular_functionphosphoenolpyruvate carboxylase activity
C0009735biological_processresponse to cytokinin
C0010167biological_processresponse to nitrate
C0015977biological_processcarbon fixation
C0015979biological_processphotosynthesis
C0016829molecular_functionlyase activity
C0048366biological_processleaf development
C0060359biological_processresponse to ammonium ion
D0003824molecular_functioncatalytic activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006099biological_processtricarboxylic acid cycle
D0008964molecular_functionphosphoenolpyruvate carboxylase activity
D0009735biological_processresponse to cytokinin
D0010167biological_processresponse to nitrate
D0015977biological_processcarbon fixation
D0015979biological_processphotosynthesis
D0016829molecular_functionlyase activity
D0048366biological_processleaf development
D0060359biological_processresponse to ammonium ion
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue GLY A 1001
ChainResidue
ATRP333
AARG334
BSER100
BPHE225
BARG226
BTHR227
BGLU229
BLEU938

site_idAC2
Number of Residues4
Detailsbinding site for residue ACT A 1002
ChainResidue
ASER602
AGLY640
AGLN673
AGLY600

site_idAC3
Number of Residues5
Detailsbinding site for residue ACT A 1003
ChainResidue
AHIS177
AGLU566
AASP603
AARG759
AARG773

site_idAC4
Number of Residues4
Detailsbinding site for residue ACT A 1004
ChainResidue
ATYR601
AALA614
AGLN621
ASER658

site_idAC5
Number of Residues8
Detailsbinding site for residue GLY B 1001
ChainResidue
BHIS177
BARG456
BGLU566
BSER602
BASP603
BARG759
BARG773
BALA774

site_idAC6
Number of Residues5
Detailsbinding site for residue GLY B 1002
ChainResidue
APHE225
ATHR227
AGLU229
BTRP333
BARG334

site_idAC7
Number of Residues2
Detailsbinding site for residue ACT B 1003
ChainResidue
BARG183
BSER185

site_idAC8
Number of Residues5
Detailsbinding site for residue ACT B 1004
ChainResidue
BHIS177
BGLY600
BSER602
BGLY640
BGLN673

site_idAC9
Number of Residues5
Detailsbinding site for residue ACT B 1005
ChainResidue
BTYR601
BALA614
BGLN621
BSER658
BGLN659

site_idAD1
Number of Residues5
Detailsbinding site for residue GLY C 1001
ChainResidue
CTRP333
CARG334
DPHE225
DASP228
DGLU229

site_idAD2
Number of Residues7
Detailsbinding site for residue ACT C 1002
ChainResidue
CTYR601
CALA614
CLEU617
CGLN621
CARG641
CSER658
CGLN659

site_idAD3
Number of Residues3
Detailsbinding site for residue ACT C 1003
ChainResidue
CARG183
CSER185
DARG372

site_idAD4
Number of Residues7
Detailsbinding site for residue ACT C 1004
ChainResidue
CARG456
CGLY600
CTYR601
CSER602
CGLY640
CGLN673
CACT1005

site_idAD5
Number of Residues5
Detailsbinding site for residue ACT C 1005
ChainResidue
CHIS177
CASP603
CARG759
CARG773
CACT1004

site_idAD6
Number of Residues5
Detailsbinding site for residue GLY D 1001
ChainResidue
CSER100
CPHE225
CGLU229
DTRP333
DARG334

site_idAD7
Number of Residues4
Detailsbinding site for residue ACT D 1002
ChainResidue
CGLU369
CARG372
DARG183
DSER185

site_idAD8
Number of Residues6
Detailsbinding site for residue ACT D 1003
ChainResidue
DMET598
DGLY600
DTYR601
DSER602
DGLY640
DGLN673

site_idAD9
Number of Residues7
Detailsbinding site for residue ACT D 1004
ChainResidue
DTYR601
DALA614
DTYR618
DGLN621
DARG641
DSER658
DGLN659

Functional Information from PROSITE/UniProt
site_idPS00393
Number of Residues13
DetailsPEPCASE_2 Phosphoenolpyruvate carboxylase active site 2. VMVGYSDSgKDAG
ChainResidueDetails
AVAL597-GLY609

site_idPS00781
Number of Residues12
DetailsPEPCASE_1 Phosphoenolpyruvate carboxylase active site 1. VfTAHPTQsaRR
ChainResidueDetails
AVAL173-ARG184

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:2268676
ChainResidueDetails
AHIS177
DHIS177
DLYS606
DARG647
ALYS606
AARG647
BHIS177
BLYS606
BARG647
CHIS177
CLYS606
CARG647

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:16668168
ChainResidueDetails
ASER15
BSER15
CSER15
DSER15

225158

PDB entries from 2024-09-18

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