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6GNI

Cryo-tomography and subtomogram averaging of Sar1-Sec23-Sec24 - fitted model.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0003400biological_processregulation of COPII vesicle coating
A0005096molecular_functionGTPase activator activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0006886biological_processintracellular protein transport
A0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
A0008270molecular_functionzinc ion binding
A0012507cellular_componentER to Golgi transport vesicle membrane
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0016192biological_processvesicle-mediated transport
A0016236biological_processmacroautophagy
A0030127cellular_componentCOPII vesicle coat
A0031410cellular_componentcytoplasmic vesicle
A0046872molecular_functionmetal ion binding
A0061709biological_processreticulophagy
A0070863biological_processpositive regulation of protein exit from endoplasmic reticulum
A0070971cellular_componentendoplasmic reticulum exit site
A0090110biological_processCOPII-coated vesicle cargo loading
A0090114biological_processCOPII-coated vesicle budding
A1902953biological_processpositive regulation of ER to Golgi vesicle-mediated transport
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0006886biological_processintracellular protein transport
E0006886biological_processintracellular protein transport
E0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
E0008270molecular_functionzinc ion binding
E0030127cellular_componentCOPII vesicle coat
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 801
ChainResidue
ACYS56
ACYS61
ACYS80
ACYS83

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN E 1001
ChainResidue
ECYS231
ECYS234
ECYS253
ECYS256

site_idAC3
Number of Residues18
Detailsbinding site for residue GNP B 201
ChainResidue
BASP32
BASN33
BALA34
BGLY35
BLYS36
BTHR37
BTHR38
BPRO53
BTHR54
BGLY76
BASN132
BLYS133
BASP135
BSER172
BVAL173
BVAL174
BMG202
AARG722

site_idAC4
Number of Residues3
Detailsbinding site for residue MG B 202
ChainResidue
BTHR37
BTHR54
BGNP201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
BGLY30
BASP73
BASN132
ECYS256

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198
ChainResidueDetails
BTHR155

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
BSER157

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
BLYS133

222036

PDB entries from 2024-07-03

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