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6YK0

Crystal structure of mouse pyridoxal kinase in complex with ATP-gamma-S

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005524molecular_functionATP binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0008478molecular_functionpyridoxal kinase activity
A0008614biological_processpyridoxine metabolic process
A0009443biological_processpyridoxal 5'-phosphate salvage
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0030170molecular_functionpyridoxal phosphate binding
A0030955molecular_functionpotassium ion binding
A0031402molecular_functionsodium ion binding
A0031403molecular_functionlithium ion binding
A0042803molecular_functionprotein homodimerization activity
A0042817biological_processpyridoxal metabolic process
A0042818biological_processpyridoxamine metabolic process
A0042822biological_processpyridoxal phosphate metabolic process
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0005524molecular_functionATP binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0008478molecular_functionpyridoxal kinase activity
B0008614biological_processpyridoxine metabolic process
B0009443biological_processpyridoxal 5'-phosphate salvage
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0030170molecular_functionpyridoxal phosphate binding
B0030955molecular_functionpotassium ion binding
B0031402molecular_functionsodium ion binding
B0031403molecular_functionlithium ion binding
B0042803molecular_functionprotein homodimerization activity
B0042817biological_processpyridoxal metabolic process
B0042818biological_processpyridoxamine metabolic process
B0042822biological_processpyridoxal phosphate metabolic process
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0005524molecular_functionATP binding
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0008270molecular_functionzinc ion binding
C0008478molecular_functionpyridoxal kinase activity
C0008614biological_processpyridoxine metabolic process
C0009443biological_processpyridoxal 5'-phosphate salvage
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
C0030170molecular_functionpyridoxal phosphate binding
C0030955molecular_functionpotassium ion binding
C0031402molecular_functionsodium ion binding
C0031403molecular_functionlithium ion binding
C0042803molecular_functionprotein homodimerization activity
C0042817biological_processpyridoxal metabolic process
C0042818biological_processpyridoxamine metabolic process
C0042822biological_processpyridoxal phosphate metabolic process
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0005524molecular_functionATP binding
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0008270molecular_functionzinc ion binding
D0008478molecular_functionpyridoxal kinase activity
D0008614biological_processpyridoxine metabolic process
D0009443biological_processpyridoxal 5'-phosphate salvage
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
D0030170molecular_functionpyridoxal phosphate binding
D0030955molecular_functionpotassium ion binding
D0031402molecular_functionsodium ion binding
D0031403molecular_functionlithium ion binding
D0042803molecular_functionprotein homodimerization activity
D0042817biological_processpyridoxal metabolic process
D0042818biological_processpyridoxamine metabolic process
D0042822biological_processpyridoxal phosphate metabolic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue PG4 A 401
ChainResidue
APHE43
ATHR47
ATYR84
BARG224

site_idAC2
Number of Residues15
Detailsbinding site for residue AGS A 402
ChainResidue
ASER187
AMET223
AARG224
ALYS225
AVAL226
AALA228
ATHR233
AGLY234
AMET263
ALEU267
AASP113
AASP118
AASN150
AGLU153
ATHR186

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 403
ChainResidue
AGLU4
ACYS5
ALEU31
AGLY32
ALYS247

site_idAC4
Number of Residues2
Detailsbinding site for residue PG4 A 404
ChainResidue
AARG6
AASP78

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL A 405
ChainResidue
AHIS63
ATYR66
AGLU67
AMET93
AASP96
AGLU100

site_idAC6
Number of Residues1
Detailsbinding site for residue EDO A 406
ChainResidue
AGLY159

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 407
ChainResidue
AASN39
AGLN42
BASN39
BGLN42

site_idAC8
Number of Residues16
Detailsbinding site for residue AGS B 401
ChainResidue
BASP113
BVAL115
BASP118
BASN150
BGLU153
BTHR186
BSER187
BMET223
BARG224
BVAL226
BALA228
BTHR233
BGLY234
BMET263
BLEU267
BEDO409

site_idAC9
Number of Residues1
Detailsbinding site for residue EDO B 402
ChainResidue
BARG272

site_idAD1
Number of Residues5
Detailsbinding site for residue GOL B 403
ChainResidue
BCYS5
BLEU31
BGLY32
BPHE33
BHIS246

site_idAD2
Number of Residues2
Detailsbinding site for residue EDO B 404
ChainResidue
BHIS46
BTHR47

site_idAD3
Number of Residues3
Detailsbinding site for residue EDO B 405
ChainResidue
BGLU155
BLEU156
BGLY159

site_idAD4
Number of Residues3
Detailsbinding site for residue EDO B 406
ChainResidue
BSER106
BLEU108
BASP145

site_idAD5
Number of Residues1
Detailsbinding site for residue EDO B 407
ChainResidue
BASP302

site_idAD6
Number of Residues5
Detailsbinding site for residue EDO B 408
ChainResidue
BSER40
BVAL56
BLEU57
BTHR85
BPHE90

site_idAD7
Number of Residues2
Detailsbinding site for residue EDO B 409
ChainResidue
BLEU199
BAGS401

site_idAD8
Number of Residues14
Detailsbinding site for residue AGS C 401
ChainResidue
CASP113
CGLY117
CASP118
CASN150
CGLU153
CTHR186
CSER187
CMET223
CARG224
CVAL226
CALA228
CTHR233
CGLY234
CLEU267

site_idAD9
Number of Residues4
Detailsbinding site for residue EDO C 402
ChainResidue
CLYS102
CPRO142
CASP145
CGLY179

site_idAE1
Number of Residues5
Detailsbinding site for residue GOL C 403
ChainResidue
CHIS63
CGLU67
CMET93
CILE97
CGLU100

site_idAE2
Number of Residues2
Detailsbinding site for residue EDO C 404
ChainResidue
CTHR47
CPHE43

site_idAE3
Number of Residues3
Detailsbinding site for residue EDO C 405
ChainResidue
CLEU31
CGLY32
CEDO406

site_idAE4
Number of Residues4
Detailsbinding site for residue EDO C 406
ChainResidue
CLEU31
CPHE33
CALA243
CEDO405

site_idAE5
Number of Residues5
Detailsbinding site for residue EDO C 407
ChainResidue
CARG86
CTYR127
CVAL128
CPRO129
CGLN130

site_idAE6
Number of Residues4
Detailsbinding site for residue EDO C 408
ChainResidue
CASN39
CGLN42
DASN39
DGLN42

site_idAE7
Number of Residues14
Detailsbinding site for residue AGS D 401
ChainResidue
DVAL115
DASP118
DASN150
DGLU153
DTHR186
DSER187
DMET223
DARG224
DVAL226
DALA228
DTHR233
DGLY234
DPHE237
DLEU267

site_idAE8
Number of Residues2
Detailsbinding site for residue EDO D 402
ChainResidue
DHIS46
DTHR47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"O00764","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues56
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O00764","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O00764","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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