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3A37

Structural insight into the membrane insertion of tail-anchored proteins by Get3

Functional Information from GO Data
ChainGOidnamespacecontents
A0000750biological_processpheromone-dependent signal transduction involved in conjugation with cellular fusion
A0005085molecular_functionguanyl-nucleotide exchange factor activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006457biological_processprotein folding
A0006620biological_processpost-translational protein targeting to endoplasmic reticulum membrane
A0006890biological_processretrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
A0008270molecular_functionzinc ion binding
A0009408biological_processresponse to heat
A0010038biological_processresponse to metal ion
A0016192biological_processvesicle-mediated transport
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0034599biological_processcellular response to oxidative stress
A0042802molecular_functionidentical protein binding
A0043529cellular_componentGET complex
A0044183molecular_functionprotein folding chaperone
A0045048biological_processprotein insertion into ER membrane
A0046685biological_processresponse to arsenic-containing substance
A0046872molecular_functionmetal ion binding
A0051082molecular_functionunfolded protein binding
A0071816biological_processtail-anchored membrane protein insertion into ER membrane
B0000750biological_processpheromone-dependent signal transduction involved in conjugation with cellular fusion
B0005085molecular_functionguanyl-nucleotide exchange factor activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0006457biological_processprotein folding
B0006620biological_processpost-translational protein targeting to endoplasmic reticulum membrane
B0006890biological_processretrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
B0008270molecular_functionzinc ion binding
B0009408biological_processresponse to heat
B0010038biological_processresponse to metal ion
B0016192biological_processvesicle-mediated transport
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0034599biological_processcellular response to oxidative stress
B0042802molecular_functionidentical protein binding
B0043529cellular_componentGET complex
B0044183molecular_functionprotein folding chaperone
B0045048biological_processprotein insertion into ER membrane
B0046685biological_processresponse to arsenic-containing substance
B0046872molecular_functionmetal ion binding
B0051082molecular_functionunfolded protein binding
B0071816biological_processtail-anchored membrane protein insertion into ER membrane
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP A 400
ChainResidue
AGLY27
APRO315
ALEU316
ACYS317
AGLY319
AGLU320
AILE321
AARG322
AGLY28
AVAL29
AGLY30
ALYS31
ATHR32
ATHR33
AASN272
AGLN273

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP B 401
ChainResidue
BGLY27
BVAL29
BGLY30
BLYS31
BTHR32
BTHR33
BASN272
BPRO315
BLEU316
BCYS317
BGLY319
BILE321
BPHE330

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 363
ChainResidue
ACYS285
ACYS288
BCYS285
BCYS288

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AASP57
BASP57

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ALYS26
AGLU245
AASN272
APRO315
BLYS26
BGLU245
BASN272
BPRO315

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03112, ECO:0000269|PubMed:19675567
ChainResidueDetails
ACYS285
ACYS288
BCYS285
BCYS288

221716

PDB entries from 2024-06-26

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