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2DDW

Crystal Structure of Pyridoxal Kinase from the Escherichia coli PdxK gene complexed with pyridoxal at 3.2 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0030170molecular_functionpyridoxal phosphate binding
A0036172biological_processthiamine salvage
A0042803molecular_functionprotein homodimerization activity
A0042816biological_processvitamin B6 metabolic process
A0046872molecular_functionmetal ion 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
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 Residues4
DetailsBINDING SITE FOR RESIDUE PXL A 1003
ChainResidue
ASER23
APRO58
AHIS59
AASP233

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PXL B 1005
ChainResidue
BSER23
BPRO58
BHIS59
BASP233

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16740960, ECO:0007744|PDB:2DDW
ChainResidueDetails
ASER23
AHIS59
AASP233
BSER23
BHIS59
BASP233

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:16740960, ECO:0007744|PDB:2DDO
ChainResidueDetails
AASP125
BTHR231
ATHR157
ATHR195
AHIS221
ATHR231
BASP125
BTHR157
BTHR195
BHIS221

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:16740960
ChainResidueDetails
ATYR136
BTYR136

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16740960
ChainResidueDetails
AGLU162
BGLU162

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 2024-11-13

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