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1JDE

K22A mutant of pyruvate, phosphate dikinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0006090biological_processpyruvate metabolic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0046872molecular_functionmetal ion binding
A0050242molecular_functionpyruvate, phosphate dikinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 901
ChainResidue
AGLU361
AARG523
ATRP527

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 902
ChainResidue
AMET99
APRO100
AGLY101
AMET102
AMET103
AARG337

Functional Information from PROSITE/UniProt
site_idPS00370
Number of Residues12
DetailsPEP_ENZYMES_PHOS_SITE PEP-utilizing enzymes phosphorylation site signature. GGmTsHAAVVAR
ChainResidueDetails
AGLY450-ARG461

site_idPS00742
Number of Residues19
DetailsPEP_ENZYMES_2 PEP-utilizing enzymes signature 2. EfFSFGTNDLtQMTFGfsR
ChainResidueDetails
AGLU761-ARG779

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:11468288
ChainResidueDetails
AALA456

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:7857929, ECO:0000305|PubMed:8610096
ChainResidueDetails
AGLY832

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
ASER93

site_idSWS_FT_FI4
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:8610096
ChainResidueDetails
ATHR562
ATYR618
AILE746
ATHR767
AASN768
AASP769
ALEU770

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PDRP1 => ECO:0000250
ChainResidueDetails
ASER454

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1kc7
ChainResidueDetails
AHIS455
ACYS831

site_idMCSA1
Number of Residues9
DetailsM-CSA 207
ChainResidueDetails
AALA22electrostatic stabiliser, hydrogen bond donor
AARG92electrostatic stabiliser, hydrogen bond donor
AGLY101electrostatic stabiliser, hydrogen bond donor
AMET103electrostatic stabiliser, hydrogen bond donor
AARG337electrostatic stabiliser, hydrogen bond donor
AHIS455covalently attached, nucleofuge, nucleophile, polar interaction
ASER764hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
ACYS831hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
ATYR851hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

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PDB entries from 2025-06-11

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