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1S3G

Crystal structure of adenylate kinase from Bacillus globisporus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
A0008270molecular_functionzinc ion binding
A0009165biological_processnucleotide biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase 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
A0046872molecular_functionmetal ion binding
A0046940biological_processnucleoside monophosphate phosphorylation
A0050145molecular_functionnucleoside monophosphate kinase activity
A1901566biological_processorganonitrogen compound biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 219
ChainResidue
ACYS130
ACYS133
ACYS150
AASP153

site_idAC2
Number of Residues34
DetailsBINDING SITE FOR RESIDUE AP5 A 218
ChainResidue
AGLY14
ATHR15
ATHR31
AGLY32
AARG36
AMET53
AALA57
ALEU58
AVAL59
ATHR64
AGLY85
APHE86
AARG88
AGLN92
AARG123
AARG127
ASER136
ATYR137
AHIS138
AASN142
AARG160
AARG171
ALYS199
AILE201
AHOH223
AHOH224
AHOH234
AHOH237
AHOH251
APRO9
AGLY10
AALA11
AGLY12
ALYS13

Functional Information from PROSITE/UniProt
site_idPS00113
Number of Residues12
DetailsADENYLATE_KINASE Adenylate kinase signature. FLLDGFPRtvpQ
ChainResidueDetails
APHE81-GLN92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:15100224
ChainResidueDetails
AGLY10
ASER136
ACYS150
AASP153
AARG160
AARG171
ALYS199
ATHR31
AARG36
AALA57
AGLY85
AGLN92
AARG127
ACYS130
ACYS133

218853

PDB entries from 2024-04-24

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