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4JLP

Crystal structure of R150K aquifex adenylate kinase mutant

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 Residues22
DetailsBINDING SITE FOR RESIDUE ADP A 301
ChainResidue
AGLY10
ATYR134
AHIS135
ALYS189
APRO190
AVAL191
AADP302
AHOH403
AHOH416
AHOH423
AHOH493
AALA11
AHOH498
AHOH531
BARG55
AGLY12
ALYS13
AGLY14
ATHR15
AARG120
AARG124
AVAL133

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ADP A 302
ChainResidue
APRO9
ATHR31
AGLY32
ALEU35
AARG36
AMET53
AGLU57
AVAL59
AILE64
AGLY82
AARG85
AGLN89
AARG124
AARG161
AADP301
AHOH411
AHOH412
AHOH415
AHOH426
AHOH431
AHOH435
AHOH498
AHOH513
AHOH549
AHOH692

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ADP B 301
ChainResidue
BTHR31
BGLY32
BLEU35
BARG36
BMET53
BGLU57
BLEU58
BVAL59
BILE64
BGLY82
BARG85
BGLN89
BARG124
BARG161
BHOH401
BHOH404
BHOH406
BHOH411
BHOH431
BHOH453
BHOH477
BHOH506
BHOH763

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ADP B 302
ChainResidue
BGLY10
BALA11
BGLY12
BLYS13
BGLY14
BTHR15
BARG120
BARG124
BTYR134
BHIS135
BTYR138
BLYS189
BPRO190
BVAL191
BHOH405
BHOH431
BHOH445
BHOH447
BHOH452
BHOH506
BHOH518
BHOH767

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
AGLY10
ALYS189
BGLY10
BTHR31
BGLU57
BGLY82
BGLN89
BARG120
BARG124
BVAL133
BARG161
ATHR31
BLYS189
AGLU57
AGLY82
AGLN89
AARG120
AARG124
AVAL133
AARG161

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PDB entries from 2024-11-06

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