Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1HUR

HUMAN ADP-RIBOSYLATION FACTOR 1 COMPLEXED WITH GDP, FULL LENGTH NON-MYRISTOYLATED

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000139	cellular_component	Golgi membrane
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0002090	biological_process	regulation of receptor internalization
A	0003723	molecular_function	RNA binding
A	0003924	molecular_function	GTPase activity
A	0003925	molecular_function	G protein activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005794	cellular_component	Golgi apparatus
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005925	cellular_component	focal adhesion
A	0006878	biological_process	intracellular copper ion homeostasis
A	0006886	biological_process	intracellular protein transport
A	0012505	cellular_component	endomembrane system
A	0014069	cellular_component	postsynaptic density
A	0015031	biological_process	protein transport
A	0016192	biological_process	vesicle-mediated transport
A	0016787	molecular_function	hydrolase activity
A	0019904	molecular_function	protein domain specific binding
A	0030017	cellular_component	sarcomere
A	0031252	cellular_component	cell leading edge
A	0032991	cellular_component	protein-containing complex
A	0034315	biological_process	regulation of Arp2/3 complex-mediated actin nucleation
A	0043005	cellular_component	neuron projection
A	0045202	cellular_component	synapse
A	0060292	biological_process	long-term synaptic depression
A	0070062	cellular_component	extracellular exosome
A	0097061	biological_process	dendritic spine organization
A	0098586	biological_process	cellular response to virus
A	1990386	biological_process	mitotic cleavage furrow ingression
B	0000139	cellular_component	Golgi membrane
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0002090	biological_process	regulation of receptor internalization
B	0003723	molecular_function	RNA binding
B	0003924	molecular_function	GTPase activity
B	0003925	molecular_function	G protein activity
B	0005515	molecular_function	protein binding
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0005794	cellular_component	Golgi apparatus
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0005925	cellular_component	focal adhesion
B	0006878	biological_process	intracellular copper ion homeostasis
B	0006886	biological_process	intracellular protein transport
B	0012505	cellular_component	endomembrane system
B	0014069	cellular_component	postsynaptic density
B	0015031	biological_process	protein transport
B	0016192	biological_process	vesicle-mediated transport
B	0016787	molecular_function	hydrolase activity
B	0019904	molecular_function	protein domain specific binding
B	0030017	cellular_component	sarcomere
B	0031252	cellular_component	cell leading edge
B	0032991	cellular_component	protein-containing complex
B	0034315	biological_process	regulation of Arp2/3 complex-mediated actin nucleation
B	0043005	cellular_component	neuron projection
B	0045202	cellular_component	synapse
B	0060292	biological_process	long-term synaptic depression
B	0070062	cellular_component	extracellular exosome
B	0097061	biological_process	dendritic spine organization
B	0098586	biological_process	cellular response to virus
B	1990386	biological_process	mitotic cleavage furrow ingression

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 182

Chain	Residue
A	GDP1
A	THR31
A	GLU54
A	HOH443
A	HOH452
A	HOH466
A	HOH505

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG B 182

Chain	Residue
B	GLU54
B	HOH411
B	HOH423
B	HOH476
B	HOH500
B	GDP1
B	THR31

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE GDP A 1

Chain	Residue
A	ASP26
A	ALA27
A	ALA28
A	GLY29
A	LYS30
A	THR31
A	THR32
A	ASN126
A	LYS127
A	ASP129
A	LEU130
A	CYS159
A	ALA160
A	MG182
A	HOH443
A	HOH449
A	HOH466
B	GLY50
B	ASN52

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GDP B 1

Chain	Residue
A	GLY50
A	ASN52
B	ALA27
B	ALA28
B	GLY29
B	LYS30
B	THR31
B	THR32
B	ASN126
B	LYS127
B	ASP129
B	LEU130
B	CYS159
B	ALA160
B	THR161
B	MG182
B	HOH410
B	HOH411
B	HOH476
B	HOH477
B	HOH493

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	26
Details	Region: {"description":"Important for the stable binding to the membranes","evidences":[{"source":"UniProtKB","id":"P84080","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7990966","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HUR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N-acetylglycine; alternate","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Lipidation: {"description":"N-myristoyl glycine; alternate","evidences":[{"source":"PubMed","id":"20213681","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23535599","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25255805","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25807930","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
A	GLN71

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
B	GLN71

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)