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4JKY

Cobalt between two ADP's in the active site of 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
A0043231cellular_componentintracellular membrane-bounded organelle
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
B0043231cellular_componentintracellular membrane-bounded organelle
B0044209biological_processAMP salvage
B0046940biological_processnucleoside monophosphate phosphorylation
B0050145molecular_functionnucleoside monophosphate kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues20
Details
ChainResidue
AGLY10
ATYR134
AHIS135
ATYR138
ALYS189
APRO190
AVAL191
AADP302
AHOH401
AHOH437
AHOH475
AALA11
AHOH482
AGLY12
ALYS13
AGLY14
ATHR15
AARG120
AARG124
AVAL133

site_idAC2
Number of Residues22
Details
ChainResidue
APRO9
ATHR31
AGLY32
ALEU35
AARG36
AMET53
AGLU57
AVAL59
AILE64
AGLY82
AARG85
AGLN89
AARG124
AARG150
AARG161
AADP301
AHOH401
AHOH407
AHOH408
AHOH412
AHOH413
AHOH422

site_idAC3
Number of Residues17
Details
ChainResidue
BGLY10
BALA11
BGLY12
BLYS13
BGLY14
BTHR15
BARG120
BARG124
BTYR134
BHIS135
BTYR138
BLYS189
BPRO190
BVAL191
BADP302
BHOH401
BHOH429

site_idAC4
Number of Residues23
Details
ChainResidue
BPRO9
BTHR31
BGLY32
BLEU35
BARG36
BMET53
BGLU57
BVAL59
BILE64
BGLY82
BARG85
BGLN89
BARG124
BARG150
BARG161
BADP301
BHOH401
BHOH404
BHOH408
BHOH415
BHOH442
BHOH458
BHOH460

Functional Information from PROSITE/UniProt
site_idPS00113
Number of Residues12
DetailsADENYLATE_KINASE Adenylate kinase signature. VIFDGFPRtvkQ
ChainResidueDetails
AVAL78-GLN89

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:18026086
ChainResidueDetails
AGLN89
AARG120
AARG124
AVAL133
AARG161
ALYS189
BGLY10
BTHR31
BGLU57
BGLY82
BGLN89
BARG120
BARG124
BVAL133
BARG161
BLYS189
AGLY10
ATHR31
AGLU57
AGLY82

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PDB entries from 2024-06-12

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