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

2FA9

The crystal structure of Sar1[H79G]-GDP provides insight into the coat-controlled GTP hydrolysis in the disassembly of COP II

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005765cellular_componentlysosomal membrane
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006886biological_processintracellular protein transport
A0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0016192biological_processvesicle-mediated transport
A0016787molecular_functionhydrolase activity
A0030127cellular_componentCOPII vesicle coat
A0032368biological_processregulation of lipid transport
A0032580cellular_componentGolgi cisterna membrane
A0042953biological_processlipoprotein transport
A0046872molecular_functionmetal ion binding
A0048208biological_processCOPII vesicle coating
A0055088biological_processlipid homeostasis
A0070971cellular_componentendoplasmic reticulum exit site
A0090110biological_processCOPII-coated vesicle cargo loading
A0140353biological_processlipid export from cell
A0140785molecular_functionamino acid sensor activity
A1903432biological_processregulation of TORC1 signaling
A1904262biological_processnegative regulation of TORC1 signaling
A1990253biological_processcellular response to leucine starvation
B0000166molecular_functionnucleotide binding
B0003924molecular_functionGTPase activity
B0003925molecular_functionG protein activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005764cellular_componentlysosome
B0005765cellular_componentlysosomal membrane
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0006886biological_processintracellular protein transport
B0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0016192biological_processvesicle-mediated transport
B0016787molecular_functionhydrolase activity
B0030127cellular_componentCOPII vesicle coat
B0032368biological_processregulation of lipid transport
B0032580cellular_componentGolgi cisterna membrane
B0042953biological_processlipoprotein transport
B0046872molecular_functionmetal ion binding
B0048208biological_processCOPII vesicle coating
B0055088biological_processlipid homeostasis
B0070971cellular_componentendoplasmic reticulum exit site
B0090110biological_processCOPII-coated vesicle cargo loading
B0140353biological_processlipid export from cell
B0140785molecular_functionamino acid sensor activity
B1903432biological_processregulation of TORC1 signaling
B1904262biological_processnegative regulation of TORC1 signaling
B1990253biological_processcellular response to leucine starvation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1003
ChainResidue
BTHR39
BGDP1001
BHOH2058
BHOH2059
BHOH2060

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 1004
ChainResidue
AHOH2044
AHOH2063
AHOH2064
ATHR39
APRO59
AGDP1002
AHOH2004

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 2001
ChainResidue
BPHE18
BGLY185
BGLY187
BGLU188
BARG191
BHOH2038
BHOH2039

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 2002
ChainResidue
APHE18
AGLN184
AGLY185
ATYR186
AGLY187
AGLU188
AARG191
AHOH2006
AHOH2055

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GDP B 1001
ChainResidue
BASP34
BASN35
BALA36
BGLY37
BLYS38
BTHR39
BTHR40
BASP75
BASN134
BLYS135
BASP137
BARG138
BSER179
BVAL180
BLEU181
BMG1003
BHOH2026
BHOH2035
BHOH2059
BHOH2060

site_idAC6
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GDP A 1002
ChainResidue
AASP34
AASN35
AALA36
AGLY37
ALYS38
ATHR39
ATHR40
AASP75
AASN134
ALYS135
AASP137
AARG138
ASER179
AVAL180
ALEU181
AMG1004
AHOH2009
AHOH2017
AHOH2044
AHOH2059
AHOH2063

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11739406, ECO:0007744|PDB:1F6B
ChainResidueDetails
AASP34
AALA36
AASP75
BASP34
BALA36
BASP75

site_idSWS_FT_FI2
Number of Residues22
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9Y6B6
ChainResidueDetails
AASN35
AVAL180
ALEU181
BASN35
BGLY37
BLYS38
BTHR39
BTHR40
BHIS58
BASN134
BLYS135
AGLY37
BASP137
BVAL180
BLEU181
ALYS38
ATHR39
ATHR40
AHIS58
AASN134
ALYS135
AASP137

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Y6B6
ChainResidueDetails
ASER164
BSER164

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
BGLY79

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon