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3GMT

Crystal structure of adenylate kinase from burkholderia pseudomallei

Functional Information from GO Data
ChainGOidnamespacecontents
A0004017molecular_functionadenylate kinase activity
A0004127molecular_functioncytidylate kinase activity
A0004550molecular_functionnucleoside diphosphate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006225biological_processUDP biosynthetic process
A0009123biological_processnucleoside monophosphate metabolic process
A0009165biological_processnucleotide biosynthetic process
A0016301molecular_functionkinase activity
A0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
A0019205molecular_functionnucleobase-containing compound kinase activity
A0033862molecular_functionUMP kinase activity
A0044209biological_processAMP salvage
A0046705biological_processCDP biosynthetic process
A0046940biological_processnucleoside monophosphate phosphorylation
A0050145molecular_functionnucleoside monophosphate kinase activity
B0004017molecular_functionadenylate kinase activity
B0004127molecular_functioncytidylate kinase activity
B0004550molecular_functionnucleoside diphosphate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006139biological_processnucleobase-containing compound metabolic process
B0006225biological_processUDP biosynthetic process
B0009123biological_processnucleoside monophosphate metabolic process
B0009165biological_processnucleotide biosynthetic process
B0016301molecular_functionkinase activity
B0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
B0019205molecular_functionnucleobase-containing compound kinase activity
B0033862molecular_functionUMP kinase activity
B0044209biological_processAMP salvage
B0046705biological_processCDP biosynthetic process
B0046940biological_processnucleoside monophosphate phosphorylation
B0050145molecular_functionnucleoside monophosphate kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AGLY10
AALA11
AGLY12
ALYS13
AGLY14
AHOH322

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AARG119
AMSE120
AARG123

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 301
ChainResidue
BGLY10
BALA11
BGLY12
BLYS13
BGLY14

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BARG119
BMSE120
BARG123

Functional Information from PROSITE/UniProt
site_idPS00113
Number of Residues12
DetailsADENYLATE_KINASE Adenylate kinase signature. YLFDGFPRtiaQ
ChainResidueDetails
ATYR81-GLN92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235
ChainResidueDetails
AGLY10
AARG167
AGLY206
BGLY10
BTHR31
BARG36
BLYS57
BGLY85
BGLN92
BARG123
BTHR132
ATHR31
BARG156
BARG167
BGLY206
AARG36
ALYS57
AGLY85
AGLN92
AARG123
ATHR132
AARG156

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1zio
ChainResidueDetails
ALYS13
AARG156
AARG123
AARG167
AASP158
AASP159

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1zio
ChainResidueDetails
BLYS13
BARG156
BARG123
BARG167
BASP158
BASP159

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1zio
ChainResidueDetails
ALYS13
AARG123
AASP33
AASP159

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1zio
ChainResidueDetails
BLYS13
BARG123
BASP33
BASP159

219515

PDB entries from 2024-05-08

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