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1NN3

Crystal structure of human thymidylate kinase with d4TMP + ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004550molecular_functionnucleoside diphosphate kinase activity
A0004798molecular_functionthymidylate kinase activity
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006227biological_processdUDP biosynthetic process
A0006233biological_processdTDP biosynthetic process
A0006235biological_processdTTP biosynthetic process
A0009165biological_processnucleotide biosynthetic process
A0016301molecular_functionkinase activity
A0043627biological_processresponse to estrogen
A0045445biological_processmyoblast differentiation
A0046105biological_processthymidine biosynthetic process
A0046686biological_processresponse to cadmium ion
A0046940biological_processnucleoside monophosphate phosphorylation
A0071363biological_processcellular response to growth factor stimulus
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
ASER20
AADP302
AHOH504
AHOH505
AHOH506
AHOH507

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AHOH502
AHOH503
AHOH503
AHOH501
AHOH501
AHOH502

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 2DT A 301
ChainResidue
APHE42
AARG45
ALEU57
APHE72
AARG76
AARG97
AGLY102
APHE105
ATYR151
AHOH504
AHOH507
AHOH526
AHOH552
AHOH634
AHOH659
AHOH711
AHOH732

site_idAC4
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ADP A 302
ChainResidue
AARG16
AALA17
AGLY18
ALYS19
ASER20
ATHR21
AARG143
ALYS182
ASER183
AILE184
AARG192
AMG401
AHOH504
AHOH506
AHOH507
AHOH520
AHOH535
AHOH566
AHOH573
AHOH583
AHOH592
AHOH602
AHOH626
AHOH670
AHOH677

Functional Information from PROSITE/UniProt
site_idPS01331
Number of Residues13
DetailsTHYMIDYLATE_KINASE Thymidylate kinase signature. VVDRYafSGvAFT
ChainResidueDetails
AVAL94-THR106

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12614151, ECO:0007744|PDB:1NMX, ECO:0007744|PDB:1NMY, ECO:0007744|PDB:1NN0, ECO:0007744|PDB:1NN3
ChainResidueDetails
AARG16

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12614151, ECO:0007744|PDB:1NMY, ECO:0007744|PDB:1NMZ, ECO:0007744|PDB:1NN1
ChainResidueDetails
AARG97

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1NMX, ECO:0007744|PDB:1NMY, ECO:0007744|PDB:1NN0, ECO:0007744|PDB:1NN3
ChainResidueDetails
ALYS182

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1NMY, ECO:0007744|PDB:1NMZ, ECO:0007744|PDB:1NN1, ECO:0007744|PDB:1NN5
ChainResidueDetails
AARG192

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330
ChainResidueDetails
AALA2

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS169

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PDB entries from 2024-07-24

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