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5LU4

C4-type pyruvate phosphate dikinase: conformational intermediate of central domain in the swiveling mechanism

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006090biological_processpyruvate metabolic process
A0009507cellular_componentchloroplast
A0015979biological_processphotosynthesis
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0046872molecular_functionmetal ion binding
A0050242molecular_functionpyruvate, phosphate dikinase activity
B0003824molecular_functioncatalytic activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006090biological_processpyruvate metabolic process
B0009507cellular_componentchloroplast
B0015979biological_processphotosynthesis
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0046872molecular_functionmetal ion binding
B0050242molecular_functionpyruvate, phosphate dikinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue ADP A 901
ChainResidue
ALYS25
AGLU280
AGLU324
ALEU335
AGLN336
AMG902
ASER93
AARG95
ATHR108
ALEU110
ASER242
AMET243
AVAL244
AGLY279

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 902
ChainResidue
AGLU324
AGLN336
AADP901

site_idAC3
Number of Residues9
Detailsbinding site for residue PYR A 903
ChainResidue
ALEU560
AARG619
AGLU748
AGLY769
ATHR770
AASN771
AASP772
AMG904
AHOH1001

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 904
ChainResidue
AARG619
AASP622
AARG669
AGLU748
AASP772
APYR903

site_idAC5
Number of Residues15
Detailsbinding site for residue ADP B 901
ChainResidue
BLYS25
BSER93
BARG95
BTHR108
BLEU110
BGLN241
BSER242
BMET243
BVAL244
BGLY279
BGLU280
BGLU324
BLEU335
BGLN336
BMG902

site_idAC6
Number of Residues3
Detailsbinding site for residue MG B 902
ChainResidue
BGLU324
BGLN336
BADP901

site_idAC7
Number of Residues5
Detailsbinding site for residue MG B 903
ChainResidue
BARG619
BASP622
BARG669
BGLU748
BASP772

Functional Information from PROSITE/UniProt
site_idPS00370
Number of Residues12
DetailsPEP_ENZYMES_PHOS_SITE PEP-utilizing enzymes phosphorylation site signature. GGmTsHAAVVAR
ChainResidueDetails
AGLY451-ARG462

site_idPS00742
Number of Residues19
DetailsPEP_ENZYMES_2 PEP-utilizing enzymes signature 2. DfFSFGTNDLtQMTFGysR
ChainResidueDetails
AASP764-ARG782

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000250|UniProtKB:P11155
ChainResidueDetails
AHIS456
BHIS456

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P11155
ChainResidueDetails
ACYS834
BCYS834

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P11155
ChainResidueDetails
AARG562
BGLU748
BGLY769
BTHR770
BASN771
BASP772
AARG619
AGLU748
AGLY769
ATHR770
AASN771
AASP772
BARG562
BARG619

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PDRP1 => ECO:0000250
ChainResidueDetails
ATHR454
BTHR454

222624

PDB entries from 2024-07-17

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