Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8RSR

Crystal structure of marine actinobacteria clade rhodopsin (MAR) - human GTPase Arf1 (L8K,Q71L) chimera; N state

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 SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:7990966, ECO:0007744|PDB:1HUR
ChainResidueDetails
AGLY240

site_idSWS_FT_FI2
Number of Residues1
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
AASN342

site_idSWS_FT_FI3
Number of Residues1
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
AALA376

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylglycine; alternate => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
AGLY218

site_idSWS_FT_FI5
Number of Residues1
DetailsLIPID: N-myristoyl glycine; alternate => ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:23535599, ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:25807930
ChainResidueDetails
AGLY218

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon