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1ZIN

ADENYLATE KINASE WITH BOUND AP5A

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
A0008270molecular_functionzinc ion binding
A0009123biological_processnucleoside monophosphate metabolic process
A0009132biological_processnucleoside diphosphate metabolic process
A0009165biological_processnucleotide biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
A0019205molecular_functionnucleobase-containing compound kinase activity
A0044209biological_processAMP salvage
A0046872molecular_functionmetal ion binding
A0046940biological_processnucleoside monophosphate phosphorylation
A0050145molecular_functionnucleoside monophosphate kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 219
ChainResidue
ACYS130
ACYS133
ACYS150
ACYS153

site_idAC2
Number of Residues36
DetailsBINDING SITE FOR RESIDUE AP5 A 218
ChainResidue
AGLY14
ATHR15
ATHR31
APHE35
AARG36
AMET53
AASP57
AVAL59
ATHR64
AGLY85
AARG88
AGLN92
AARG123
ALEU124
AARG127
ATYR137
AHIS138
AHIS142
AARG160
AARG171
AGLN199
AMET201
AHOH300
AHOH301
AHOH306
AHOH309
AHOH311
AHOH352
AHOH355
AHOH426
AHOH532
APRO9
AGLY10
AALA11
AGLY12
ALYS13

Functional Information from PROSITE/UniProt
site_idPS00113
Number of Residues12
DetailsADENYLATE_KINASE Adenylate kinase signature. FLLDGFPRtvaQ
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:9715904
ChainResidueDetails
AGLY10
ATHR136
ACYS150
ACYS153
AARG160
AARG171
AGLN199
ATHR31
AARG36
AASP57
AGLY85
AGLN92
AARG127
ACYS130
ACYS133

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1zio
ChainResidueDetails
ALYS13
AARG127
AARG171
AARG160
AASP162
AASP163

site_idMCSA1
Number of Residues5
DetailsM-CSA 290
ChainResidueDetails
ALYS13electrostatic stabiliser
AARG88attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
AARG127attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
AARG160attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
AARG171electrostatic stabiliser

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PDB entries from 2024-10-30

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