Q60175: Protein translocase subunit SecY (secY)

Protein translocase subunit SecY (secY) is a 436-residue protein from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q60175.

Gene
secY
Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Length
436 residues
Mean pLDDT
85.1
Model
AF-Q60175-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.1 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate46%
70 to 90Confident: backbone generally right40%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions2%

What pLDDT means and how to read it

Function

The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently

Subunit structure

Component of the Sec protein translocase complex. Heterotrimer consisting of alpha (SecY), beta (SecG) and gamma (SecE) subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. May interact with SecDF, and other proteins may be involved

Subcellular location

Cell membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
1RH5X-ray3.2 ÅA=1-436
1RHZX-ray3.5 ÅA=1-436
2YXQX-ray3.5 ÅA=1-436
2YXRX-ray3.6 ÅA=1-436
3DKNEM8.7 ÅA=2-433
4V4NEM9.0 ÅAX=1-436
3BO0EM9.6 ÅA=2-433
3BO1EM9.6 ÅA=2-433
4V7IEMA=2-433

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