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6YK1

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

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0030170molecular_functionpyridoxal phosphate binding
A0030955molecular_functionpotassium ion binding
A0031402molecular_functionsodium ion binding
A0031403molecular_functionlithium ion binding
A0036094molecular_functionsmall molecule binding
A0042803molecular_functionprotein homodimerization activity
A0042816biological_processvitamin B6 metabolic process
A0042817biological_processpyridoxal metabolic process
A0042818biological_processpyridoxamine metabolic process
A0042822biological_processpyridoxal phosphate metabolic process
A0042823biological_processpyridoxal phosphate biosynthetic process
A0043066biological_processnegative regulation of apoptotic process
A0046872molecular_functionmetal ion binding
A0070280molecular_functionpyridoxal binding
A0097159molecular_functionorganic cyclic compound 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
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0030170molecular_functionpyridoxal phosphate binding
B0030955molecular_functionpotassium ion binding
B0031402molecular_functionsodium ion binding
B0031403molecular_functionlithium ion binding
B0036094molecular_functionsmall molecule binding
B0042803molecular_functionprotein homodimerization activity
B0042816biological_processvitamin B6 metabolic process
B0042817biological_processpyridoxal metabolic process
B0042818biological_processpyridoxamine metabolic process
B0042822biological_processpyridoxal phosphate metabolic process
B0042823biological_processpyridoxal phosphate biosynthetic process
B0043066biological_processnegative regulation of apoptotic process
B0046872molecular_functionmetal ion binding
B0070280molecular_functionpyridoxal binding
B0097159molecular_functionorganic cyclic compound 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
C0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
C0030170molecular_functionpyridoxal phosphate binding
C0030955molecular_functionpotassium ion binding
C0031402molecular_functionsodium ion binding
C0031403molecular_functionlithium ion binding
C0036094molecular_functionsmall molecule binding
C0042803molecular_functionprotein homodimerization activity
C0042816biological_processvitamin B6 metabolic process
C0042817biological_processpyridoxal metabolic process
C0042818biological_processpyridoxamine metabolic process
C0042822biological_processpyridoxal phosphate metabolic process
C0042823biological_processpyridoxal phosphate biosynthetic process
C0043066biological_processnegative regulation of apoptotic process
C0046872molecular_functionmetal ion binding
C0070280molecular_functionpyridoxal binding
C0097159molecular_functionorganic cyclic compound 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
D0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
D0030170molecular_functionpyridoxal phosphate binding
D0030955molecular_functionpotassium ion binding
D0031402molecular_functionsodium ion binding
D0031403molecular_functionlithium ion binding
D0036094molecular_functionsmall molecule binding
D0042803molecular_functionprotein homodimerization activity
D0042816biological_processvitamin B6 metabolic process
D0042817biological_processpyridoxal metabolic process
D0042818biological_processpyridoxamine metabolic process
D0042822biological_processpyridoxal phosphate metabolic process
D0042823biological_processpyridoxal phosphate biosynthetic process
D0043066biological_processnegative regulation of apoptotic process
D0046872molecular_functionmetal ion binding
D0070280molecular_functionpyridoxal binding
D0097159molecular_functionorganic cyclic compound binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue GOL A 501
ChainResidue
APRO191

site_idAC2
Number of Residues2
Detailsbinding site for residue PG4 A 502
ChainResidue
AGLY159
AEDO505

site_idAC3
Number of Residues6
Detailsbinding site for residue D95 A 503
ChainResidue
APHE43
ATHR47
ATYR84
AARG86
AASP87
AEDO512

site_idAC4
Number of Residues13
Detailsbinding site for residue AGS A 504
ChainResidue
AASP113
AASP118
ATHR148
AASN150
AGLU153
ATHR186
ASER187
AMET223
AVAL226
AALA228
ATHR233
AGLY234
ALEU267

site_idAC5
Number of Residues1
Detailsbinding site for residue EDO A 505
ChainResidue
APG4502

site_idAC6
Number of Residues7
Detailsbinding site for residue EDO A 506
ChainResidue
AASN75
ALYS76
ATYR77
ALEU101
AGLN104
AASN105
AEDO513

site_idAC7
Number of Residues7
Detailsbinding site for residue EDO A 507
ChainResidue
AGLN11
ALEU81
ATHR82
AGLY83
AASP113
AASP235
AALA238

site_idAC8
Number of Residues4
Detailsbinding site for residue EDO A 508
ChainResidue
AHIS46
ATHR47
AVAL231
AHOH603

site_idAC9
Number of Residues2
Detailsbinding site for residue EDO A 509
ChainResidue
ALYS119
AGLY124

site_idAD1
Number of Residues4
Detailsbinding site for residue EDO A 510
ChainResidue
AHIS63
AGLU67
AMET93
AGLU100

site_idAD2
Number of Residues2
Detailsbinding site for residue EDO A 511
ChainResidue
AVAL30
BLYS297

site_idAD3
Number of Residues4
Detailsbinding site for residue EDO A 512
ChainResidue
ATRP52
AGLY54
AD95503
BVAL306

site_idAD4
Number of Residues3
Detailsbinding site for residue EDO A 513
ChainResidue
ATYR77
AASP78
AEDO506

site_idAD5
Number of Residues4
Detailsbinding site for residue EDO A 514
ChainResidue
ACYS5
ALEU31
AGLY32
ALYS247

site_idAD6
Number of Residues1
Detailsbinding site for residue EDO A 515
ChainResidue
ATHR182

site_idAD7
Number of Residues5
Detailsbinding site for residue GOL B 402
ChainResidue
BCYS5
BLEU31
BGLY32
BPHE33
BHIS246

site_idAD8
Number of Residues15
Detailsbinding site for residue AGS B 403
ChainResidue
BASP113
BASP118
BTHR148
BASN150
BGLU153
BTHR186
BSER187
BMET223
BARG224
BVAL226
BALA228
BTHR233
BGLY234
BLEU267
BHOH514

site_idAD9
Number of Residues5
Detailsbinding site for residue EDO B 404
ChainResidue
AASN72
BALA50
BSER285
BPRO286
BALA287

site_idAE1
Number of Residues3
Detailsbinding site for residue EDO B 405
ChainResidue
BSER12
BTHR47
BEDO406

site_idAE2
Number of Residues3
Detailsbinding site for residue EDO B 406
ChainResidue
BPHE43
BTYR84
BEDO405

site_idAE3
Number of Residues4
Detailsbinding site for residue EDO B 407
ChainResidue
AASN39
AGLN42
BASN39
BGLN42

site_idAE4
Number of Residues4
Detailsbinding site for residue EDO B 408
ChainResidue
BGLU100
BHIS63
BMET93
BASP96

site_idAE5
Number of Residues3
Detailsbinding site for residue EDO C 501
ChainResidue
CGLN104
CSER106
CARG107

site_idAE6
Number of Residues2
Detailsbinding site for residue GOL C 503
ChainResidue
CTHR47
CHOH605

site_idAE7
Number of Residues5
Detailsbinding site for residue GOL C 504
ChainResidue
CLYS102
CPRO142
CALA144
CASP145
CGLY179

site_idAE8
Number of Residues15
Detailsbinding site for residue AGS C 505
ChainResidue
CASP113
CGLY117
CASP118
CASN150
CGLU153
CTHR186
CSER187
CARG224
CVAL226
CALA228
CTHR233
CGLY234
CMET263
CLEU267
CHOH614

site_idAE9
Number of Residues2
Detailsbinding site for residue EDO C 506
ChainResidue
CHIS51
CTRP52

site_idAF1
Number of Residues1
Detailsbinding site for residue EDO C 507
ChainResidue
CGLU166

site_idAF2
Number of Residues3
Detailsbinding site for residue EDO C 508
ChainResidue
CCYS5
CLEU31
CLYS247

site_idAF3
Number of Residues6
Detailsbinding site for residue EDO C 509
ChainResidue
CSER40
CVAL56
CLEU57
CTHR85
CARG86
CPHE90

site_idAF4
Number of Residues5
Detailsbinding site for residue EDO C 510
ChainResidue
CLYS76
CTYR77
CLEU101
CGLN104
CASN105

site_idAF5
Number of Residues3
Detailsbinding site for residue EDO C 511
ChainResidue
CHIS63
CMET93
CGLU100

site_idAF6
Number of Residues4
Detailsbinding site for residue EDO D 401
ChainResidue
CASN39
CGLN42
DASN39
DGLN42

site_idAF7
Number of Residues16
Detailsbinding site for residue AGS D 402
ChainResidue
DASP113
DVAL115
DASP118
DTYR127
DTHR148
DASN150
DGLU153
DTHR186
DSER187
DVAL226
DALA228
DTHR233
DGLY234
DPHE237
DMET263
DLEU267

site_idAF8
Number of Residues3
Detailsbinding site for residue EDO D 403
ChainResidue
DLEU31
DGLY32
DPHE33

site_idAF9
Number of Residues3
Detailsbinding site for residue EDO D 404
ChainResidue
DPHE43
DHIS46
DTHR47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:O00764
ChainResidueDetails
AASP235
BASP235
CASP235
DASP235

site_idSWS_FT_FI2
Number of Residues40
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O00764
ChainResidueDetails
ATHR148
AASN150
ATHR186
AVAL226
ATHR233
AGLY234
BSER12
BTHR47
BASP113
BASP118
BTHR148
BASN150
BTHR186
BVAL226
BTHR233
BGLY234
CSER12
CTHR47
CASP113
CASP118
CTHR148
CASN150
CTHR186
CVAL226
CTHR233
CGLY234
DSER12
DTHR47
DASP113
DASP118
DTHR148
DASN150
DTHR186
DVAL226
DTHR233
DGLY234
ATHR47
AASP113
AASP118
ASER12

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P82197
ChainResidueDetails
DMET1
AMET1
BMET1
CMET1

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
BSER59
CSER59
DSER59
ASER59

site_idSWS_FT_FI5
Number of Residues12
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O00764
ChainResidueDetails
BSER213
BSER285
CSER164
CSER213
CSER285
DSER164
DSER213
DSER285
ASER213
ASER285
BSER164
ASER164

221051

PDB entries from 2024-06-12

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