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1U81

Delta-17 Human ADP Ribosylation Factor 1 Complexed with GDP

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
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
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 2
ChainResidue
AGLU54

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GDP A 1
ChainResidue
ALYS127
ALEU25
AALA27
AALA28
AGLY29
ALYS30
ATHR31
ATHR32
AASN126

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7990966","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HUR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
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 Residues1
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

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

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AALA27

239149

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