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3GMT

Crystal structure of adenylate kinase from burkholderia pseudomallei

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004017molecular_functionAMP kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006139biological_processnucleobase-containing compound metabolic process
A0009165biological_processnucleotide biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
A0019205molecular_functionnucleobase-containing compound kinase activity
A0044209biological_processAMP salvage
A0046940biological_processnucleoside monophosphate phosphorylation
B0000166molecular_functionnucleotide binding
B0004017molecular_functionAMP kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006139biological_processnucleobase-containing compound metabolic process
B0009165biological_processnucleotide biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
B0019205molecular_functionnucleobase-containing compound kinase activity
B0044209biological_processAMP salvage
B0046940biological_processnucleoside monophosphate phosphorylation
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 Residues74
DetailsRegion: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20331978","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues33
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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

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PDB entries from 2025-12-24

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