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4NU0

Crystal structure of Adenylate kinase from Streptococcus pneumoniae with Ap5A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004017molecular_functionadenylate kinase activity
A0004127molecular_functioncytidylate kinase activity
A0004550molecular_functionnucleoside diphosphate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006225biological_processUDP biosynthetic process
A0009123biological_processnucleoside monophosphate metabolic process
A0009165biological_processnucleotide biosynthetic process
A0016301molecular_functionkinase activity
A0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
A0019205molecular_functionnucleobase-containing compound kinase activity
A0033862molecular_functionUMP kinase activity
A0044209biological_processAMP salvage
A0046705biological_processCDP biosynthetic process
A0046940biological_processnucleoside monophosphate phosphorylation
A0050145molecular_functionnucleoside monophosphate kinase activity
B0004017molecular_functionadenylate kinase activity
B0004127molecular_functioncytidylate kinase activity
B0004550molecular_functionnucleoside diphosphate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006139biological_processnucleobase-containing compound metabolic process
B0006225biological_processUDP biosynthetic process
B0009123biological_processnucleoside monophosphate metabolic process
B0009165biological_processnucleotide biosynthetic process
B0016301molecular_functionkinase activity
B0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
B0019205molecular_functionnucleobase-containing compound kinase activity
B0033862molecular_functionUMP kinase activity
B0044209biological_processAMP salvage
B0046705biological_processCDP biosynthetic process
B0046940biological_processnucleoside monophosphate phosphorylation
B0050145molecular_functionnucleoside monophosphate kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
AAP5302
AHOH402
AHOH416
AHOH442
AHOH452

site_idAC2
Number of Residues40
DetailsBINDING SITE FOR RESIDUE AP5 A 302
ChainResidue
ALYS13
AGLY14
ATHR15
ATHR31
AGLY32
APHE35
AARG36
AILE53
AGLU57
AVAL59
ATHR64
AGLY86
ATYR87
AARG89
AGLN93
AARG124
AARG128
ATHR137
APHE138
AHIS139
APHE142
AARG156
AARG167
AGLN195
AILE197
AMG301
AHOH402
AHOH404
AHOH416
AHOH432
AHOH442
AHOH482
AHOH521
AHOH539
AHOH587
AHOH591
APRO9
AGLY10
AALA11
AGLY12

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 301
ChainResidue
BAP5302
BHOH405
BHOH501
BHOH554
BHOH593

site_idAC4
Number of Residues42
DetailsBINDING SITE FOR RESIDUE AP5 B 302
ChainResidue
BPRO9
BGLY10
BALA11
BGLY12
BLYS13
BGLY14
BTHR15
BTHR31
BGLY32
BPHE35
BARG36
BILE53
BGLU57
BLEU58
BVAL59
BTHR64
BGLY86
BTYR87
BARG89
BGLN93
BARG124
BLEU125
BARG128
BTHR137
BPHE138
BHIS139
BPHE142
BARG156
BARG167
BGLN195
BILE197
BMG301
BHOH404
BHOH405
BHOH419
BHOH426
BHOH481
BHOH553
BHOH554
BHOH558
BHOH574
BHOH593

Functional Information from PROSITE/UniProt
site_idPS00113
Number of Residues12
DetailsADENYLATE_KINASE Adenylate kinase signature. FLLDGYPRtieQ
ChainResidueDetails
APHE82-GLN93

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235
ChainResidueDetails
AGLY86
AGLN93
AARG128
ATHR137
AARG156
AARG167
AGLN195
BGLY10
BTHR31
BARG36
BGLU57
BGLY86
BGLN93
BARG128
BTHR137
BARG156
BARG167
BGLN195
AGLY10
ATHR31
AARG36
AGLU57

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PDB entries from 2024-05-15

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