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3EG9

Crystal structure of the mammalian COPII-coat protein Sec23/24 bound to the transport signal sequence of membrin

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 800
ChainResidue
ACYS61
ACYS66
ACYS85
ACYS88

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B1100
ChainResidue
BCYS364
BCYS367
BCYS386
BCYS389

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:3EFO, ECO:0007744|PDB:3EG9, ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYX
ChainResidueDetails
BARG363
BARG366
BGLN385
BPHE388

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER267

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ATHR308

227344

PDB entries from 2024-11-13

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