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5VNI

Crystal structure of Sec23a/Sec24a/Sec22 complexed with a C-terminal FA sorting motif

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0005096molecular_functionGTPase activator activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
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
A0030127cellular_componentCOPII vesicle coat
A0030134cellular_componentCOPII-coated ER to Golgi transport vesicle
A0031410cellular_componentcytoplasmic vesicle
A0046872molecular_functionmetal ion binding
A0048471cellular_componentperinuclear region of cytoplasm
A0070971cellular_componentendoplasmic reticulum exit site
A0072659biological_processprotein localization to plasma membrane
A0090110biological_processCOPII-coated vesicle cargo loading
A0090114biological_processCOPII-coated vesicle budding
B0006886biological_processintracellular protein transport
B0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
B0008270molecular_functionzinc ion binding
B0030127cellular_componentCOPII vesicle coat
C0005484molecular_functionSNAP receptor activity
C0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
C0006890biological_processretrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 801
ChainResidue
ACYS61
ACYS66
ACYS85
ACYS88

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN B 1101
ChainResidue
BCYS431
BCYS434
BCYS452
BCYS455

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O75396
ChainResidueDetails
CLYS38
BCYS434
BCYS452
BCYS455

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079
ChainResidueDetails
CSER137

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O75396
ChainResidueDetails
CTHR140

218853

PDB entries from 2024-04-24

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