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1J2J

Crystal structure of GGA1 GAT N-terminal region in complex with ARF1 GTP form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0002090biological_processregulation of receptor internalization
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005770cellular_componentlate endosome
A0005778cellular_componentperoxisomal membrane
A0005794cellular_componentGolgi apparatus
A0005802cellular_componenttrans-Golgi network
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006878biological_processintracellular copper ion homeostasis
A0006886biological_processintracellular protein transport
A0007015biological_processactin filament organization
A0012505cellular_componentendomembrane system
A0014069cellular_componentpostsynaptic density
A0015031biological_processprotein transport
A0016192biological_processvesicle-mediated transport
A0016787molecular_functionhydrolase activity
A0019003molecular_functionGDP binding
A0019904molecular_functionprotein domain specific binding
A0030017cellular_componentsarcomere
A0030137cellular_componentCOPI-coated vesicle
A0031252cellular_componentcell leading edge
A0032991cellular_componentprotein-containing complex
A0034315biological_processregulation of Arp2/3 complex-mediated actin nucleation
A0034379biological_processvery-low-density lipoprotein particle assembly
A0043005cellular_componentneuron projection
A0045202cellular_componentsynapse
A0045807biological_processpositive regulation of endocytosis
A0045956biological_processpositive regulation of calcium ion-dependent exocytosis
A0050714biological_processpositive regulation of protein secretion
A0055108biological_processGolgi to transport vesicle transport
A0060292biological_processlong-term synaptic depression
A0060999biological_processpositive regulation of dendritic spine development
A0070142biological_processsynaptic vesicle budding
A0097061biological_processdendritic spine organization
A0097212biological_processlysosomal membrane organization
A0098586biological_processcellular response to virus
A0098974biological_processpostsynaptic actin cytoskeleton organization
A0098978cellular_componentglutamatergic synapse
A1902307biological_processpositive regulation of sodium ion transmembrane transport
A1902824biological_processpositive regulation of late endosome to lysosome transport
A1902953biological_processpositive regulation of ER to Golgi vesicle-mediated transport
A1903725biological_processregulation of phospholipid metabolic process
A1990386biological_processmitotic cleavage furrow ingression
A1990583molecular_functionphospholipase D activator activity
B0005802cellular_componenttrans-Golgi network
B0006886biological_processintracellular protein transport
B0031267molecular_functionsmall GTPase binding
B0035091molecular_functionphosphatidylinositol binding
B0043130molecular_functionubiquitin binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1002
ChainResidue
ATHR31
ATHR48
AGTP1001
AHOH1021
AHOH1022

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 1
ChainResidue
ATRP66

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 2
ChainResidue
BARG180

site_idAC4
Number of Residues26
DetailsBINDING SITE FOR RESIDUE GTP A 1001
ChainResidue
AALA28
AGLY29
ALYS30
ATHR31
ATHR32
ATHR45
ATHR48
AGLY69
AGLY70
AASN126
ALYS127
AASP129
ALEU130
AALA160
AMG1002
AHOH1015
AHOH1017
AHOH1018
AHOH1021
AHOH1022
AHOH1025
AHOH1093
AHOH1094
AHOH1095
AASP26
AALA27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12679809","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O3Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2J59","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1O3Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2J59","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
ALEU71

243531

PDB entries from 2025-10-22

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