Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1E9D

Mutant human thymidylate kinase (F105Y) complexed with AZTMP and 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
AHOH2026
AHOH2187
AHOH2188
AHOH2192

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AHOH2109
AHOH2110
AHOH2110
AHOH2051
AHOH2051
AHOH2109

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATM A 301
ChainResidue
APHE42
APHE72
AARG76
AARG97
AGLY102
ATYR105
ATYR151
AGLN157
AHOH2100
AHOH2135
AHOH2138
AHOH2186
AHOH2187
AHOH2188
AHOH2189
AHOH2190
AHOH2191

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ADP A 302
ChainResidue
AARG16
AALA17
AGLY18
ALYS19
ASER20
ATHR21
AARG143
ALYS182
ASER183
AILE184
AARG192
AMG401
AHOH2028
AHOH2100
AHOH2153
AHOH2187
AHOH2188
AHOH2192
AHOH2193
AHOH2194
AHOH2195
AHOH2197
AHOH2198
AHOH2199

Functional Information from PROSITE/UniProt
site_idPS01331
Number of Residues13
DetailsTHYMIDYLATE_KINASE Thymidylate kinase signature. VVDRYafSGvAYT
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

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon