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2YXU

Human Pyridoxal Kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0008478molecular_functionpyridoxal kinase activity
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
A0034774cellular_componentsecretory granule lumen
A0035580cellular_componentspecific granule lumen
A0042803molecular_functionprotein homodimerization activity
A0042816biological_processvitamin B6 metabolic process
A0042817biological_processpyridoxal metabolic process
A0042818biological_processpyridoxamine metabolic process
A0042822biological_processpyridoxal phosphate metabolic process
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
B0000287molecular_functionmagnesium ion binding
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0008478molecular_functionpyridoxal kinase activity
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
B0034774cellular_componentsecretory granule lumen
B0035580cellular_componentspecific granule lumen
B0042803molecular_functionprotein homodimerization activity
B0042816biological_processvitamin B6 metabolic process
B0042817biological_processpyridoxal metabolic process
B0042818biological_processpyridoxamine metabolic process
B0042822biological_processpyridoxal phosphate metabolic process
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 1404
ChainResidue
AASP118
AHOH1506
AHOH1507

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 1406
ChainResidue
AASP113
ATHR148
ATHR186
AHOH1508

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 2404
ChainResidue
BHOH2412
BASP118
BHOH2411

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA B 2406
ChainResidue
BTHR148
BTHR186
BHOH2413

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 1501
ChainResidue
ACYS5
ALEU31
AGLY32

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 B 1517
ChainResidue
BLEU31
BGLY32
BHIS246

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 B 1527
ChainResidue
BGLN63
BGLU100

site_idAC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP A 1410
ChainResidue
AASP113
AASP118
ATYR127
AASN150
AGLU153
ATHR186
ASER187
AARG224
ALYS225
AALA228
ATHR233
AGLY234
ALEU267
AHOH1506
AHOH1507
AHOH1510

site_idAC9
Number of Residues21
DetailsBINDING SITE FOR RESIDUE ATP B 2410
ChainResidue
BASP113
BASP118
BTYR127
BTHR148
BASN150
BGLU153
BTHR186
BSER187
BLEU199
BARG224
BLYS225
BALA228
BTHR233
BGLY234
BLEU263
BLEU267
BHOH2411
BHOH2412
BHOH2419
BHOH2500
BHOH2540

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 1011
ChainResidue
ATYR66
AARG70
AMET93
AGLU100

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 1013
ChainResidue
ASER12
AHIS46
ATHR47
ATYR84
AHOH1602

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MPD B 1015
ChainResidue
BPRO142
BALA144
BASP145
BGLY179
BPRO180
BASP181
BHOH2438
BHOH2466

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD B 1019
ChainResidue
BSER12
BHIS46
BTHR47
BASP235
BHOH2600

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MPD B 1021
ChainResidue
BASP181
BARG208

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD B 1023
ChainResidue
BSER177
BARG206
BLEU312

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD B 1025
ChainResidue
BHIS248
BPRO249
BASN250
BASN251
BHOH2546

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MPD B 1029
ChainResidue
BGLU123
BGLY124

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD B 1031
ChainResidue
APRO191
BPHE43
BTYR84
BARG86

site_idCC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MPD A 1037
ChainResidue
AASP118
AHOH1507

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD B 1039
ChainResidue
BHOH2412
BHOH2485
BHOH2500
BASP118

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD B 1041
ChainResidue
BPRO191
BHOH2441
BHOH2443

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:19351586
ChainResidueDetails
AASP235
BASP235

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19351586, ECO:0007744|PDB:3FHX
ChainResidueDetails
ASER12
BSER12

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|Ref.16, ECO:0007744|PDB:3KEU
ChainResidueDetails
ATHR47
BTHR47

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:22879864, ECO:0007744|PDB:3FHX, ECO:0007744|PDB:4EN4
ChainResidueDetails
AASP113
BASP113

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17766369, ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:22879864, ECO:0000269|Ref.16, ECO:0007744|PDB:3FHX, ECO:0007744|PDB:3KEU, ECO:0007744|PDB:4EN4
ChainResidueDetails
AASP118
BASP118

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17766369, ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:22879864, ECO:0000269|Ref.16, ECO:0007744|PDB:2YXT, ECO:0007744|PDB:3FHX, ECO:0007744|PDB:3KEU, ECO:0007744|PDB:4EN4
ChainResidueDetails
ATHR148
ATHR186
BTHR148
BTHR186

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19351586, ECO:0000269|Ref.16, ECO:0007744|PDB:3FHY, ECO:0007744|PDB:3KEU
ChainResidueDetails
AASN150
BASN150

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22879864, ECO:0000269|Ref.16, ECO:0007744|PDB:3KEU, ECO:0007744|PDB:4EN4
ChainResidueDetails
AVAL226
BVAL226

site_idSWS_FT_FI9
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17766369, ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:22879864, ECO:0000269|Ref.16, ECO:0007744|PDB:2YXU, ECO:0007744|PDB:3FHX, ECO:0007744|PDB:3FHY, ECO:0007744|PDB:3KEU, ECO:0007744|PDB:4EN4
ChainResidueDetails
ATHR233
BTHR233

site_idSWS_FT_FI10
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19351586, ECO:0000269|Ref.16, ECO:0007744|PDB:3FHX, ECO:0007744|PDB:3KEU
ChainResidueDetails
AGLY234
BGLY234

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P82197
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER59
ASER164
BSER59
BSER164

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER213
BSER213

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER285
BSER285

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1tz3
ChainResidueDetails
AGLY234
ATHR233
AGLY232
AASP235

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1tz3
ChainResidueDetails
BGLY234
BTHR233
BGLY232
BASP235

222036

PDB entries from 2024-07-03

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