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3X2S

Crystal structure of pyrene-conjugated adenylate kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004017molecular_functionadenylate kinase activity
A0004550molecular_functionnucleoside diphosphate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0009123biological_processnucleoside monophosphate metabolic process
A0009132biological_processnucleoside diphosphate metabolic process
A0009165biological_processnucleotide biosynthetic process
A0016301molecular_functionkinase activity
A0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
A0019205molecular_functionnucleobase-containing compound kinase activity
A0044209biological_processAMP salvage
A0046940biological_processnucleoside monophosphate phosphorylation
A0050145molecular_functionnucleoside monophosphate kinase activity
B0004017molecular_functionadenylate kinase activity
B0004550molecular_functionnucleoside diphosphate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006139biological_processnucleobase-containing compound metabolic process
B0009123biological_processnucleoside monophosphate metabolic process
B0009132biological_processnucleoside diphosphate metabolic process
B0009165biological_processnucleotide biosynthetic process
B0016301molecular_functionkinase activity
B0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
B0019205molecular_functionnucleobase-containing compound kinase activity
B0044209biological_processAMP salvage
B0046940biological_processnucleoside monophosphate phosphorylation
B0050145molecular_functionnucleoside monophosphate kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE JPY A 301
ChainResidue
ACYS55
ALYS166
AGLU170
AJPY302

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE JPY A 302
ChainResidue
BLEU67
BGLU70
BARG71
BGLN74
BPRO128
ACYS169
AGLU170
AGLN173
AJPY301
BMET34

site_idAC3
Number of Residues38
DetailsBINDING SITE FOR RESIDUE AP5 A 303
ChainResidue
APRO9
AGLY10
AALA11
AGLY12
ALYS13
AGLY14
ATHR15
ATHR31
AGLY32
AARG36
AMET53
ALYS57
ALEU58
AVAL59
AVAL64
AGLY85
APHE86
AARG88
AGLN92
AARG119
AARG123
AVAL132
ATYR133
AHIS134
APHE137
AARG156
AARG167
ALYS200
APRO201
AVAL202
AMG304
AHOH401
AHOH403
AHOH405
AHOH407
AHOH408
AHOH410
BGLU114

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 304
ChainResidue
AGLY14
AAP5303
AHOH401
AHOH406
AHOH407
AHOH408

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE JPY B 301
ChainResidue
AALA37
BCYS55
BLYS57
BLYS166
BJPY302

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE JPY B 302
ChainResidue
AMET34
ALEU67
AGLU70
AARG71
AGLN74
BCYS169
BGLU170
BGLN173
BJPY301

site_idAC7
Number of Residues39
DetailsBINDING SITE FOR RESIDUE AP5 B 303
ChainResidue
BARG167
BGLY198
BLYS200
BPRO201
BVAL202
BMG304
BHOH401
BHOH406
BHOH407
BHOH408
BHOH409
BHOH410
AGLU114
BPRO9
BGLY10
BALA11
BGLY12
BLYS13
BGLY14
BTHR15
BTHR31
BGLY32
BLEU35
BARG36
BLYS57
BLEU58
BVAL59
BVAL64
BGLY85
BPHE86
BARG88
BGLN92
BARG119
BARG123
BVAL132
BTYR133
BHIS134
BPHE137
BARG156

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 304
ChainResidue
BGLY14
BAP5303
BHOH401
BHOH402
BHOH406
BHOH407

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

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PDB entries from 2024-07-24

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