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7BES

CryoEM structure of Mycobacterium tuberculosis UMP Kinase (UMPK) in complex with UDP and UTP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
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
A0046940biological_processnucleoside monophosphate phosphorylation
B0000287molecular_functionmagnesium ion binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
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
B0046940biological_processnucleoside monophosphate phosphorylation
C0000287molecular_functionmagnesium ion binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005886cellular_componentplasma membrane
C0006221biological_processpyrimidine nucleotide biosynthetic process
C0006225biological_processUDP biosynthetic process
C0009041molecular_functionUMP/dUMP kinase activity
C0016301molecular_functionkinase activity
C0033862molecular_functionUMP kinase activity
C0044210biological_process'de novo' CTP biosynthetic process
C0046940biological_processnucleoside monophosphate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue UDP A 301
ChainResidue
ALYS36
AMET101
AGLY157
AMET158
ALEU160
APHE163
ASER164
ATHR165
ATHR168
AGLY38
AGLY39
AGLY77
AGLY78
APHE81
AARG82
AGLY83
AASP97

site_idAC2
Number of Residues19
Detailsbinding site for residue UDP B 301
ChainResidue
BLYS36
BGLY38
BGLY39
BGLY76
BGLY77
BGLY78
BPHE81
BARG82
BGLY83
BASP97
BGLY100
BMET101
BGLY157
BMET158
BLEU160
BPHE163
BSER164
BTHR165
BTHR168

site_idAC3
Number of Residues5
Detailsbinding site for residue UTP B 302
ChainResidue
BLEU138
BLEU140
BARG141
BARG144
BLYS148

site_idAC4
Number of Residues16
Detailsbinding site for residue UDP C 301
ChainResidue
CLYS36
CGLY39
CGLY77
CGLY78
CPHE81
CARG82
CGLY83
CASP97
CGLY100
CGLY157
CMET158
CLEU160
CTYR162
CPHE163
CTHR165
CTHR168

site_idAC5
Number of Residues15
Detailsbinding site for residue UTP C 302
ChainResidue
ALEU138
ALEU140
AARG141
AARG144
ALYS148
CARG123
CGLY131
CALA134
CGLU135
CPRO136
CARG141
CARG144
CHIS145
CLYS148
CARG150

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01220
ChainResidueDetails
ALYS36
AGLY77
AGLY78
AARG82
AASP97
AMET158
APHE191
AASP194
BLYS36
BGLY77
BGLY78
BARG82
BASP97
BMET158
BPHE191
BASP194
CLYS36
CGLY77
CGLY78
CARG82
CASP97
CMET158
CPHE191
CASP194

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609
ChainResidueDetails
ATHR2
BTHR2
CTHR2

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PDB entries from 2024-06-12

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