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1HUR

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000287molecular_functionmagnesium ion binding
A0002090biological_processregulation of receptor internalization
A0003723molecular_functionRNA binding
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
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
B0000287molecular_functionmagnesium ion binding
B0002090biological_processregulation of receptor internalization
B0003723molecular_functionRNA binding
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
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 Residues7
DetailsBINDING SITE FOR RESIDUE MG A 182
ChainResidue
AGDP1
ATHR31
AGLU54
AHOH443
AHOH452
AHOH466
AHOH505

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 182
ChainResidue
BGLU54
BHOH411
BHOH423
BHOH476
BHOH500
BGDP1
BTHR31

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GDP A 1
ChainResidue
AASP26
AALA27
AALA28
AGLY29
ALYS30
ATHR31
ATHR32
AASN126
ALYS127
AASP129
ALEU130
ACYS159
AALA160
AMG182
AHOH443
AHOH449
AHOH466
BGLY50
BASN52

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP B 1
ChainResidue
AGLY50
AASN52
BALA27
BALA28
BGLY29
BLYS30
BTHR31
BTHR32
BASN126
BLYS127
BASP129
BLEU130
BCYS159
BALA160
BTHR161
BMG182
BHOH410
BHOH411
BHOH476
BHOH477
BHOH493

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:7990966, ECO:0007744|PDB:1HUR
ChainResidueDetails
ALEU25
BLEU25

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14690595, ECO:0000269|PubMed:15308674, ECO:0000269|PubMed:7990966, ECO:0000269|Ref.34, ECO:0007744|PDB:1HUR, ECO:0007744|PDB:1RE0, ECO:0007744|PDB:1U81, ECO:0007744|PDB:3O47
ChainResidueDetails
ALYS127
BLYS127

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15308674, ECO:0000269|PubMed:7990966, ECO:0000269|Ref.34, ECO:0007744|PDB:1HUR, ECO:0007744|PDB:1RE0, ECO:0007744|PDB:3O47
ChainResidueDetails
ATHR161
BTHR161

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylglycine; alternate => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
AASN3
BASN3

site_idSWS_FT_FI5
Number of Residues2
DetailsLIPID: N-myristoyl glycine; alternate => ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:23535599, ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:25807930
ChainResidueDetails
AASN3
BASN3

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
BGLN71

223166

PDB entries from 2024-07-31

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