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3ADK

REFINED STRUCTURE OF PORCINE CYTOSOLIC ADENYLATE KINASE AT 2.1 ANGSTROMS RESOLUTION

Replaces:  2ADKReplaces:  1ADK
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
A0006172biological_processADP biosynthetic process
A0009142biological_processnucleoside triphosphate biosynthetic process
A0016301molecular_functionkinase activity
A0019205molecular_functionnucleobase-containing compound kinase activity
A0046033biological_processAMP metabolic process
A0046034biological_processATP metabolic process
A0046899molecular_functionnucleoside triphosphate adenylate kinase activity
A0046940biological_processnucleoside monophosphate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 195
ChainResidue
AGLY16
AGLY18
ASER19
AGLY20
ALYS21
AGLY22
AARG132

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 196
ChainResidue
ALEU129
AARG132
AARG138
AARG149
ALYS63
AGLN65

Functional Information from PROSITE/UniProt
site_idPS00113
Number of Residues12
DetailsADENYLATE_KINASE Adenylate kinase signature. FLIDGYPRevkQ
ChainResidueDetails
APHE90-GLN101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:2869483
ChainResidueDetails
AGLY18

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03171
ChainResidueDetails
ATHR39
AARG44
AGLN65
AGLY94
AGLN101
AARG132
AARG138
AARG149
AGLY177

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:4366177
ChainResidueDetails
AMET1

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00568
ChainResidueDetails
ASER38

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1zio
ChainResidueDetails
AARG138
ALYS21
AASP140
AARG149
AASP141
AARG132

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PDB entries from 2024-05-01

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