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3IDQ

Crystal structure of S. cerevisiae Get3 at 3.7 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
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
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
A0071816biological_processtail-anchored membrane protein insertion into ER membrane
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NI A 370
ChainResidue
AHIS367
AHIS367
AHIS367
AHIS369
AHIS369
AHIS369

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 371
ChainResidue
AHIS368
ACYS285
ACYS288
AHIS366

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03112","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19675567","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

253795

PDB entries from 2026-05-20

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