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3ASZ

CMP-complex structure of uridine kinase from Thermus thermophilus HB8

Functional Information from GO Data
ChainGOidnamespacecontents
A0004849molecular_functionuridine kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0008655biological_processpyrimidine-containing compound salvage
A0009224biological_processCMP biosynthetic process
A0016301molecular_functionkinase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0043771molecular_functioncytidine kinase activity
A0044206biological_processUMP salvage
A0044211biological_processCTP salvage
B0004849molecular_functionuridine kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0008655biological_processpyrimidine-containing compound salvage
B0009224biological_processCMP biosynthetic process
B0016301molecular_functionkinase activity
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0043771molecular_functioncytidine kinase activity
B0044206biological_processUMP salvage
B0044211biological_processCTP salvage
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE C5P A 212
ChainResidue
ATHR15
AARG142
AARG145
AARG150
AARG152
AGLN160
AHOH221
AHOH227
AHOH262
ALYS19
AASP40
ATYR43
ATYR59
AASP60
ATYR88
APHE90
ATYR93

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE C5P B 212
ChainResidue
BTHR15
BLYS19
BASP40
BTYR43
BTYR59
BASP60
BTYR88
BPHE90
BTYR93
BARG142
BARG145
BARG150
BARG152
BGLN160
BHOH229
BHOH248
BHOH262

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00551
ChainResidueDetails
AGLY13
BGLY13

222415

PDB entries from 2024-07-10

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