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3HP1

Crystal structure of human dCK R104M/D133A in complex with L-dT and ADP

Replaces:  3EXK
Functional Information from GO Data
ChainGOidnamespacecontents
A0004136molecular_functiondeoxyadenosine kinase activity
A0004137molecular_functiondeoxycytidine kinase activity
A0004138molecular_functiondeoxyguanosine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006220biological_processpyrimidine nucleotide metabolic process
A0008144molecular_functionobsolete drug binding
A0009224biological_processCMP biosynthetic process
A0016301molecular_functionkinase activity
A0019136molecular_functiondeoxynucleoside kinase activity
A0042803molecular_functionprotein homodimerization activity
A0043771molecular_functioncytidine kinase activity
A0106383biological_processdAMP salvage
A1901135biological_processcarbohydrate derivative metabolic process
A1901293biological_processnucleoside phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ADP A 301
ChainResidue
AALA31
AHIS218
AVAL238
AGLU240
AASP241
APHE242
AHOH269
AHOH281
AHOH307
AHOH329
AHOH343
AALA32
AGLY33
ALYS34
ASER35
ATHR36
AARG188
AARG192
ATYR210

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE LLT A 401
ChainResidue
AGLU53
AVAL55
AMET85
ATYR86
APHE96
AGLN97
AMET104
AARG128
AALA133
APHE137
AGLU197
AHOH263
AHOH296
AHOH307

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255
ChainResidueDetails
AGLU127

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING:
ChainResidueDetails
AGLY28
AGLU53
ATYR86
AGLN97
AARG128
AALA133
AARG188
AGLU197
AGLU240

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CK1 => ECO:0000305|PubMed:20637175
ChainResidueDetails
ASER11
ASER15

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CK1 => ECO:0000305|PubMed:20637175
ChainResidueDetails
ATHR72

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:20637175, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER74

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2ocp
ChainResidueDetails
AGLU53
AARG128

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PDB entries from 2024-07-17

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