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3AKY

STABILITY, ACTIVITY AND STRUCTURE OF ADENYLATE KINASE MUTANTS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004017molecular_functionadenylate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005758cellular_componentmitochondrial intermembrane space
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006172biological_processADP biosynthetic process
A0006270biological_processDNA replication initiation
A0009117biological_processnucleotide metabolic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
A0019205molecular_functionnucleobase-containing compound kinase activity
A0046033biological_processAMP metabolic process
A0046034biological_processATP metabolic process
A0046940biological_processnucleoside monophosphate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues40
DetailsBINDING SITE FOR RESIDUE AP5 A 301
ChainResidue
APRO13
AARG40
AMET57
AGLY61
AVAL63
AMET68
AGLY90
APHE91
AARG93
AGLN97
AARG128
AGLY14
AARG132
ASER141
ATYR142
AHIS143
APHE146
AARG165
AARG176
AGLN204
APRO205
APRO206
AALA15
AIMD302
AHOH501
AHOH504
AHOH506
AHOH517
AHOH530
AHOH536
AHOH541
AHOH570
AHOH587
AGLY16
AHOH600
ALYS17
AGLY18
ATHR19
ATHR35
AGLY36

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE IMD A 302
ChainResidue
AGLY18
AASP37
AASP89
AAP5301
AHOH541
AHOH587
AHOH621

Functional Information from PROSITE/UniProt
site_idPS00113
Number of Residues12
DetailsADENYLATE_KINASE Adenylate kinase signature. FILDGFPRtipQ
ChainResidueDetails
APHE86-GLN97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369, ECO:0000269|PubMed:8594191
ChainResidueDetails
AGLY14
AARG132
AGLN204

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369
ChainResidueDetails
ATHR35
AARG40
AGLY61
AGLY90
AGLN97
AARG165
AARG176

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369, ECO:0000269|PubMed:8594191
ChainResidueDetails
ASER141

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:3004985
ChainResidueDetails
ASER1

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PDB entries from 2024-04-24

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