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2DDO

Crystal Structure of Pyridoxal Kinase from the Escherichia coli pdxK gene at 2.6 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0008478molecular_functionpyridoxal kinase activity
A0008902molecular_functionhydroxymethylpyrimidine kinase activity
A0009443biological_processpyridoxal 5'-phosphate salvage
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0030170molecular_functionpyridoxal phosphate binding
A0036172biological_processthiamine salvage
A0042803molecular_functionprotein homodimerization activity
A0042816biological_processvitamin B6 metabolic process
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0008478molecular_functionpyridoxal kinase activity
B0008902molecular_functionhydroxymethylpyrimidine kinase activity
B0009443biological_processpyridoxal 5'-phosphate salvage
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0030170molecular_functionpyridoxal phosphate binding
B0036172biological_processthiamine salvage
B0042803molecular_functionprotein homodimerization activity
B0042816biological_processvitamin B6 metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 284
ChainResidue
ATYR136
AGLU162
AATP285

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 287
ChainResidue
BHOH361
BASP125
BTHR157
BGLU162
BGLY232
BHOH327
BHOH344

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ATP A 285
ChainResidue
AASP125
ATHR157
AASN159
AGLU162
ATHR195
AMET206
AHIS221
ASER222
AARG223
AVAL224
ATHR231
AGLY232
AMET264
AMG284
AHOH365

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16740960","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2DDW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16740960","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2DDO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16740960","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16740960","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1tz3
ChainResidueDetails
ATHR231
AASP233
AGLY232
AGLY230

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1tz3
ChainResidueDetails
BTHR231
BASP233
BGLY232
BGLY230

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PDB entries from 2025-12-17

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