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2RGX

Crystal Structure of Adenylate Kinase from Aquifex Aeolicus in complex with Ap5A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004017molecular_functionAMP 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
A0016740molecular_functiontransferase activity
A0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
A0019205molecular_functionnucleobase-containing compound kinase activity
A0044209biological_processAMP salvage
A0046940biological_processnucleoside monophosphate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 300
ChainResidue
AAP5806
AHOH881
AHOH882
AHOH883
AHOH896

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS75
AGLU129
AGLU163
AGLU167

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
AGLU91
AGLU95
AGLU98
AHOH893

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 303
ChainResidue
AHIS106
AHOH890

site_idAC5
Number of Residues41
DetailsBINDING SITE FOR RESIDUE AP5 A 806
ChainResidue
APRO9
AGLY10
AALA11
AGLY12
ALYS13
AGLY14
ATHR15
ATHR31
AGLY32
ALEU35
AMET53
AGLU57
ALEU58
AVAL59
AILE64
AGLY82
AARG85
AGLN89
AARG120
ALEU121
AARG124
AVAL133
ATYR134
AHIS135
ATYR138
AARG150
AARG161
ALYS189
APRO190
AVAL191
AZN300
AHOH810
AHOH812
AHOH825
AHOH830
AHOH833
AHOH864
AHOH881
AHOH883
AHOH896
AHOH906

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 Residues29
DetailsRegion: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18026086","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues30
DetailsRegion: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18026086","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues17
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18026086","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1zio
ChainResidueDetails
ALYS13
AASP152
AARG161
AARG124
AARG150
AASP153

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PDB entries from 2026-01-14

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