Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3ADK

REFINED STRUCTURE OF PORCINE CYTOSOLIC ADENYLATE KINASE AT 2.1 ANGSTROMS RESOLUTION

Replaces:  2ADKReplaces:  1ADK
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004017molecular_functionAMP kinase activity
A0004550molecular_functionnucleoside diphosphate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006139biological_processnucleobase-containing compound metabolic process
A0006172biological_processADP biosynthetic process
A0009142biological_processnucleoside triphosphate biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0019205molecular_functionnucleobase-containing compound kinase activity
A0046033biological_processAMP metabolic process
A0046034biological_processATP metabolic process
A0046940biological_processnucleoside monophosphate phosphorylation
A0047506molecular_functiondAMP kinase activity
A0050145molecular_functionnucleoside monophosphate kinase activity
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 Residues29
DetailsRegion: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_03171","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2832612","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4367210","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsRegion: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_03171","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2832612","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4367210","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03171","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2869483","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03171","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"HAMAP-Rule","id":"MF_03171","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4366177","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00568","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon