Structure of PDB 3ibg Chain C

Receptor sequence
>3ibgC (length=300) [Search protein sequence]
LMEPTLQSILSQKTLRWIFVGGKGGVGKTTTSCSLAIQLAKVRKSVLLIS
TDPAHNLSDAFGQKFGKEARLVDGYSNLSAMEIDPNGSIQDLLASQDLAF
SIPGVDEAMSFAEVLKQVKSLSYEVIVFDTAPTGHTLRFLQFPTVLEKAL
AKLSQLSSQFSILGARGGLPGGQNIDELLQKMESLRETISEVNTQFKNPD
MTTFVCVCIAEFLSLYETERMIQELTSYGIDTHAIVVNQLLFPGCEQCNA
RRKMQKKYLEQIEELYEDFNVVRMPLLVEEVRGKEKLEKFSEMLVHPYVP
3D structure
PDB3ibg Model for eukaryotic tail-anchored protein binding based on the structure of Get3
ChainC
Resolution3.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.-.-
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ADP C G36 G38 K39 T40 T41 N272 L314 L315 V319 R320 G25 G27 K28 T29 T30 N238 L276 L277 V281 R282
Gene Ontology
Molecular Function
GO:0005085 guanyl-nucleotide exchange factor activity
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
GO:0042802 identical protein binding
GO:0044183 protein folding chaperone
GO:0046872 metal ion binding
GO:0051082 unfolded protein binding
Biological Process
GO:0000750 pheromone-dependent signal transduction involved in conjugation with cellular fusion
GO:0006457 protein folding
GO:0006620 post-translational protein targeting to endoplasmic reticulum membrane
GO:0006890 retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
GO:0009408 response to heat
GO:0010038 response to metal ion
GO:0034599 cellular response to oxidative stress
GO:0045048 protein insertion into ER membrane
GO:0071816 tail-anchored membrane protein insertion into ER membrane
Cellular Component
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0043529 GET complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3ibg, PDBe:3ibg, PDBj:3ibg
PDBsum3ibg
PubMed19706470
UniProtQ4WY07|GET3_ASPFU ATPase get3 (Gene Name=get3)

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