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3CRC

Crystal Structure of Escherichia coli MazG, the Regulator of Nutritional Stress Response

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0006203biological_processdGTP catabolic process
A0006950biological_processresponse to stress
A0009267biological_processcellular response to starvation
A0016787molecular_functionhydrolase activity
A0046047biological_processTTP catabolic process
A0046052biological_processUTP catabolic process
A0046061biological_processdATP catabolic process
A0046076biological_processdTTP catabolic process
A0046081biological_processdUTP catabolic process
A0046872molecular_functionmetal ion binding
A0047429molecular_functionnucleoside triphosphate diphosphatase activity
A0047693molecular_functionATP diphosphatase activity
B0000166molecular_functionnucleotide binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0006203biological_processdGTP catabolic process
B0006950biological_processresponse to stress
B0009267biological_processcellular response to starvation
B0016787molecular_functionhydrolase activity
B0046047biological_processTTP catabolic process
B0046052biological_processUTP catabolic process
B0046061biological_processdATP catabolic process
B0046076biological_processdTTP catabolic process
B0046081biological_processdUTP catabolic process
B0046872molecular_functionmetal ion binding
B0047429molecular_functionnucleoside triphosphate diphosphatase activity
B0047693molecular_functionATP diphosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 264
ChainResidue
BGLU172
BGLU175
BGLU193
BASP196

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ATP B 265
ChainResidue
BTRP159
BLYS168
BGLU172
BGLU175
BLYS189
BGLU192
BASP196
ALYS222
APHE223
AARG226
ATRP253
BPHE157

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18353782
ChainResidueDetails
ALYS168
ALYS189
ALYS222
ATRP253
BLYS168
BLYS189
BLYS222
BTRP253

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AGLU172
AGLU175
AGLU193
AASP196
BGLU172
BGLU175
BGLU193
BASP196

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PDB entries from 2025-06-18

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