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1FZQ

CRYSTAL STRUCTURE OF MURINE ARL3-GDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000166molecular_functionnucleotide binding
A0000281biological_processmitotic cytokinesis
A0000287molecular_functionmagnesium ion binding
A0001822biological_processkidney development
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005813cellular_componentcentrosome
A0005819cellular_componentspindle
A0005876cellular_componentspindle microtubule
A0005881cellular_componentcytoplasmic microtubule
A0005929cellular_componentcilium
A0005930cellular_componentaxoneme
A0006892biological_processpost-Golgi vesicle-mediated transport
A0006893biological_processGolgi to plasma membrane transport
A0007224biological_processsmoothened signaling pathway
A0007264biological_processsmall GTPase-mediated signal transduction
A0008017molecular_functionmicrotubule binding
A0015031biological_processprotein transport
A0015630cellular_componentmicrotubule cytoskeleton
A0019003molecular_functionGDP binding
A0030496cellular_componentmidbody
A0032391cellular_componentphotoreceptor connecting cilium
A0035869cellular_componentciliary transition zone
A0036064cellular_componentciliary basal body
A0042073biological_processintraciliary transport
A0042461biological_processphotoreceptor cell development
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0060271biological_processcilium assembly
A0061512biological_processprotein localization to cilium
A1903441biological_processprotein localization to ciliary membrane
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
ALEU4
ASER5
AARG8
ASER39

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AHOH642
ATHR31
ALYS35
AHIS44
ALYS54
AARG149

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NH4 A 501
ChainResidue
AHIS44
AGLU141

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MES A 201
ChainResidue
AASN52
AHIS146
AVAL152
ATRP153
AGLN154
AHOH615

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE GDP A 301
ChainResidue
AASN27
AALA28
AGLY29
ALYS30
ATHR31
ATHR32
ATYR77
ASER80
AGLU83
AASN126
ALYS127
AASP129
ALEU130
ASER159
AALA160
ALEU161
AHOH524
AHOH529
AHOH536
AHOH545
AHOH553
AHOH631
AHOH649
AHOH660

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues13
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18376416","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P36405","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsLipidation: {"description":"N-myristoyl glycine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AGLN71

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PDB entries from 2026-01-21

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