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3O47

Crystal structure of ARFGAP1-ARF1 fusion protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0002090biological_processregulation of receptor internalization
A0003723molecular_functionRNA binding
A0003924molecular_functionGTPase activity
A0005096molecular_functionGTPase activator activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006878biological_processintracellular copper ion homeostasis
A0006886biological_processintracellular protein transport
A0012505cellular_componentendomembrane system
A0014069cellular_componentpostsynaptic density
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0016192biological_processvesicle-mediated transport
A0016787molecular_functionhydrolase activity
A0019904molecular_functionprotein domain specific binding
A0030017cellular_componentsarcomere
A0031252cellular_componentcell leading edge
A0032991cellular_componentprotein-containing complex
A0034315biological_processregulation of Arp2/3 complex-mediated actin nucleation
A0043005cellular_componentneuron projection
A0045202cellular_componentsynapse
A0060292biological_processlong-term synaptic depression
A0070062cellular_componentextracellular exosome
A0097061biological_processdendritic spine organization
A0098586biological_processcellular response to virus
A1990386biological_processmitotic cleavage furrow ingression
B0000139cellular_componentGolgi membrane
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0002090biological_processregulation of receptor internalization
B0003723molecular_functionRNA binding
B0003924molecular_functionGTPase activity
B0005096molecular_functionGTPase activator activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0006878biological_processintracellular copper ion homeostasis
B0006886biological_processintracellular protein transport
B0012505cellular_componentendomembrane system
B0014069cellular_componentpostsynaptic density
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0016192biological_processvesicle-mediated transport
B0016787molecular_functionhydrolase activity
B0019904molecular_functionprotein domain specific binding
B0030017cellular_componentsarcomere
B0031252cellular_componentcell leading edge
B0032991cellular_componentprotein-containing complex
B0034315biological_processregulation of Arp2/3 complex-mediated actin nucleation
B0043005cellular_componentneuron projection
B0045202cellular_componentsynapse
B0060292biological_processlong-term synaptic depression
B0070062cellular_componentextracellular exosome
B0097061biological_processdendritic spine organization
B0098586biological_processcellular response to virus
B1990386biological_processmitotic cleavage furrow ingression
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
ACYS22
ACYS25
ACYS42
ACYS45

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GDP A 502
ChainResidue
ATHR162
AASN256
ALYS257
AASP259
ALEU260
ACYS289
AALA290
ATHR291
AALA157
AALA158
AGLY159
ALYS160
ATHR161

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 501
ChainResidue
BCYS22
BCYS25
BCYS42
BCYS45

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GDP B 502
ChainResidue
BLEU155
BASP156
BALA157
BALA158
BGLY159
BLYS160
BTHR161
BTHR162
BASN256
BLYS257
BASP259
BLEU260
BCYS289
BALA290
BTHR291

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7990966","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HUR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14690595","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15308674","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7990966","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of ARFGAP1-ARF1 fusion protein.","authoringGroup":["Structural genomics consortium (SGC)."]}},{"source":"PDB","id":"1HUR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U81","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3O47","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15308674","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7990966","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of ARFGAP1-ARF1 fusion protein.","authoringGroup":["Structural genomics consortium (SGC)."]}},{"source":"PDB","id":"1HUR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3O47","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues234
DetailsDomain: {"description":"Arf-GAP","evidences":[{"source":"PROSITE-ProRule","id":"PRU00288","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues46
DetailsZinc finger: {"description":"C4-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00288","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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