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1P5Z

Structure of human dCK complexed with cytarabine and ADP-MG

Functional Information from GO Data
ChainGOidnamespacecontents
B0004136molecular_functiondeoxyadenosine kinase activity
B0004137molecular_functiondeoxycytidine kinase activity
B0004138molecular_functiondeoxyguanosine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006139biological_processnucleobase-containing compound metabolic process
B0006220biological_processpyrimidine nucleotide metabolic process
B0008144molecular_functionobsolete drug binding
B0009224biological_processCMP biosynthetic process
B0016301molecular_functionkinase activity
B0019136molecular_functiondeoxynucleoside kinase activity
B0042803molecular_functionprotein homodimerization activity
B0043771molecular_functioncytidine kinase activity
B0106383biological_processdAMP salvage
B1901135biological_processcarbohydrate derivative metabolic process
B1901293biological_processnucleoside phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BSER35
BGLU127
BADP301
BHOH575
BHOH576
BHOH577

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AR3 B 304
ChainResidue
BMET85
BTYR86
BPHE96
BGLN97
BARG128
BASP133
BPHE137
BGLU197
BHOH414
BHOH416
BILE30
BGLU53
BTRP58

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ADP B 301
ChainResidue
BALA31
BALA32
BGLY33
BLYS34
BSER35
BTHR36
BGLU127
BARG188
BARG192
BTYR210
BHIS218
BVAL238
BGLU240
BASP241
BPHE242
BMG401
BHOH418
BHOH420
BHOH422
BHOH438
BHOH454
BHOH514
BHOH550
BHOH576
BHOH577

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255
ChainResidueDetails
BGLU127

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING:
ChainResidueDetails
BGLY28
BGLU53
BTYR86
BGLN97
BARG128
BASP133
BARG188
BGLU197
BGLU240

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CK1 => ECO:0000305|PubMed:20637175
ChainResidueDetails
BSER11
BSER15

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CK1 => ECO:0000305|PubMed:20637175
ChainResidueDetails
BTHR72

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
BSER74

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2ocp
ChainResidueDetails
BGLU53
BARG128

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PDB entries from 2024-07-17

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