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2BRI

UMP KINASE FROM PYROCOCCUS FURIOSUS COMPLEXED WITH ITS SUBSTRATE ANALOG AMPPNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006225biological_processUDP biosynthetic process
A0009041molecular_functionUMP/dUMP kinase activity
A0016301molecular_functionkinase activity
A0033862molecular_functionUMP kinase activity
A0044210biological_process'de novo' CTP biosynthetic process
A0046872molecular_functionmetal ion binding
A0046940biological_processnucleoside monophosphate phosphorylation
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0006225biological_processUDP biosynthetic process
B0009041molecular_functionUMP/dUMP kinase activity
B0016301molecular_functionkinase activity
B0033862molecular_functionUMP kinase activity
B0044210biological_process'de novo' CTP biosynthetic process
B0046872molecular_functionmetal ion binding
B0046940biological_processnucleoside monophosphate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A1227
ChainResidue
AASP121
ASER182
AVAL183
AANP1226

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B1227
ChainResidue
BASP121
BSER181
BSER182
BASP185
BANP1226

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ANP A1226
ChainResidue
AGLY8
AGLY9
ASER10
AGLY43
AGLY45
ATHR120
ATHR140
AASN141
AVAL142
AGLY144
ATYR146
AALA148
AASP149
APRO150
ALYS151
ASER181
ASER182
AVAL183
AMG1227

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ANP B1226
ChainResidue
BGLY8
BGLY9
BSER10
BGLY43
BGLY44
BGLY45
BTHR140
BASN141
BGLY144
BTYR146
BALA148
BASP149
BILE170
BSER181
BSER182
BVAL183
BMG1227
BHOH2005
BHOH2006

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:16095620
ChainResidueDetails
AASP6
BGLY44
BASP66
BTHR114
BTHR120
BASP121
BGLY179
BSER182
AGLY44
AASP66
ATHR114
ATHR120
AASP121
AGLY179
ASER182
BASP6

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AGLY9
BASN141
BTYR146
BASP149
AGLY45
ATHR140
AASN141
ATYR146
AASP149
BGLY9
BGLY45
BTHR140

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG49
BARG49

219140

PDB entries from 2024-05-01

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