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4PWX

Crystal structure of an ATP-bound Get3-Get4-Get5 complex from S.cerevisiae

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
C0003674molecular_functionmolecular_function
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006620biological_processpost-translational protein targeting to endoplasmic reticulum membrane
C0016192biological_processvesicle-mediated transport
C0045048biological_processprotein insertion into ER membrane
C0072380cellular_componentTRC complex
E0003674molecular_functionmolecular_function
E0005515molecular_functionprotein binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006620biological_processpost-translational protein targeting to endoplasmic reticulum membrane
E0016192biological_processvesicle-mediated transport
E0045048biological_processprotein insertion into ER membrane
E0072380cellular_componentTRC complex
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP A 401
ChainResidue
AGLY27
AGLU320
AILE321
APHE330
AMG402
BLYS26
BGLY27
BPRO169
BGLU245
BLEU247
AGLY28
AGLY30
ALYS31
ATHR32
ATHR33
AASN61
AASN272
ALEU316

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
ALYS31
ATHR32
AASP166
AATP401

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 403
ChainResidue
ACYS285
ACYS288
BCYS285
BCYS288

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP B 401
ChainResidue
ALYS26
AGLY27
APRO169
AGLU245
ALEU247
BGLY27
BGLY28
BGLY30
BLYS31
BTHR32
BTHR33
BASN61
BASN272
BGLY319
BGLU320
BILE321
BPHE330
BMG402

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 402
ChainResidue
BTHR32
BASP166
BATP401

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AVAL57
BVAL57

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

225399

PDB entries from 2024-09-25

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