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5YCD

Crystal structure of Poecilia reticulata adenylate kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004017molecular_functionAMP kinase activity
A0004550molecular_functionnucleoside diphosphate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006139biological_processnucleobase-containing compound metabolic process
A0006172biological_processADP biosynthetic process
A0009142biological_processnucleoside triphosphate biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0019205molecular_functionnucleobase-containing compound kinase activity
A0046033biological_processAMP metabolic process
A0046034biological_processATP metabolic process
A0046940biological_processnucleoside monophosphate phosphorylation
A0047506molecular_functiondAMP kinase activity
A0050145molecular_functionnucleoside monophosphate kinase activity
B0000166molecular_functionnucleotide binding
B0004017molecular_functionAMP kinase activity
B0004550molecular_functionnucleoside diphosphate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006139biological_processnucleobase-containing compound metabolic process
B0006172biological_processADP biosynthetic process
B0009142biological_processnucleoside triphosphate biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0019205molecular_functionnucleobase-containing compound kinase activity
B0046033biological_processAMP metabolic process
B0046034biological_processATP metabolic process
B0046940biological_processnucleoside monophosphate phosphorylation
B0047506molecular_functiondAMP kinase activity
B0050145molecular_functionnucleoside monophosphate kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues41
Detailsbinding site for residue AP5 A 201
ChainResidue
AGLY16
AGLY40
ALEU43
AARG44
AMET61
AGLU65
ALEU66
AVAL67
AGLY94
ATYR95
AARG97
APRO17
AGLN101
AARG128
ALEU129
AARG132
AARG138
AARG149
ASER175
ALEU177
AVAL179
AMG202
AGLY18
AHOH301
AHOH303
AHOH307
AHOH316
AHOH321
AHOH325
AHOH332
AHOH337
AHOH357
AHOH359
ASER19
AHOH360
AHOH364
AGLY20
ALYS21
AGLY22
ATHR23
ASER39

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 202
ChainResidue
AAP5201
AHOH303
AHOH315
AHOH345
AHOH357

site_idAC3
Number of Residues42
Detailsbinding site for residue AP5 B 201
ChainResidue
AALA30
BPRO17
BGLY18
BSER19
BGLY20
BLYS21
BGLY22
BTHR23
BSER39
BGLY40
BLEU43
BARG44
BMET61
BGLU65
BVAL67
BGLY94
BTYR95
BARG97
BGLN101
BARG128
BLEU129
BARG132
BARG138
BARG149
BSER175
BLEU177
BVAL179
BMG202
BHOH301
BHOH306
BHOH314
BHOH331
BHOH335
BHOH338
BHOH345
BHOH353
BHOH364
BHOH374
BHOH381
BHOH383
BHOH385
BHOH397

site_idAC4
Number of Residues5
Detailsbinding site for residue MG B 202
ChainResidue
BAP5201
BHOH306
BHOH335
BHOH366
BHOH385

Functional Information from PROSITE/UniProt
site_idPS00113
Number of Residues12
DetailsADENYLATE_KINASE Adenylate kinase signature. FLIDGYPRevkQ
ChainResidueDetails
APHE90-GLN101

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PDB entries from 2025-12-03

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