Human TMEM175-LAMP1 full-length complex. Determined by electron microscopy at 3.5 Å resolution. Released 28 Jun 2023.
Explore 8FY5 in 3D Show helices and sheets RCSB PDB PDBe
8FY5 contains 49 α-helices and 16 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 31 | 1 | 1 |
| α-helix | 34-49 | 16 | |
| α-helix | 52-56 | 5 | |
| α-helix | 67-101 | 35 | |
| β-strand | 102 | 1 | 2 |
| β-strand | 105 | 1 | 1 |
| α-helix | 107-120 | 14 | |
| α-helix | 123-132 | 10 | |
| α-helix | 137-163 | 27 | |
| α-helix | 165-167 | 3 | |
| β-strand | 168 | 1 | 2 |
| α-helix | 170-174 | 5 | |
| α-helix | 178-189 | 12 | |
| β-strand | 255-256 | 2 | 3 |
| α-helix | 258-273 | 16 | |
| α-helix | 275-283 | 9 | |
| α-helix | 286-287 | 2 | |
| α-helix | 288-294 | 7 | |
| α-helix | 299-332 | 34 | |
| β-strand | 334 | 1 | 4 |
| β-strand | 337-338 | 2 | 3 |
| α-helix | 339-352 | 14 | |
| α-helix | 355-363 | 9 | |
| α-helix | 369-398 | 30 | |
| α-helix | 401-404 | 4 | |
| β-strand | 405 | 1 | 4 |
| α-helix | 407-409 | 3 | |
| α-helix | 416-439 | 24 | |
| α-helix | 441-443 | 3 | |
| α-helix | 444-460 | 17 | |
| α-helix | 462-475 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 31 | 1 | 5 |
| α-helix | 34-49 | 16 | |
| α-helix | 52-56 | 5 | |
| α-helix | 67-101 | 35 | |
| β-strand | 102 | 1 | 6 |
| β-strand | 105 | 1 | 5 |
| α-helix | 107-120 | 14 | |
| α-helix | 123-132 | 10 | |
| α-helix | 137-163 | 27 | |
| α-helix | 165-167 | 3 | |
| β-strand | 168 | 1 | 6 |
| α-helix | 170-174 | 5 | |
| α-helix | 178-189 | 12 | |
| β-strand | 255-256 | 2 | 7 |
| α-helix | 258-273 | 16 | |
| α-helix | 275-283 | 9 | |
| α-helix | 286-287 | 2 | |
| α-helix | 288-294 | 7 | |
| α-helix | 299-332 | 34 | |
| β-strand | 334 | 1 | 8 |
| β-strand | 337-338 | 2 | 7 |
| α-helix | 339-352 | 14 | |
| α-helix | 355-363 | 9 | |
| α-helix | 369-371 | 3 | |
| α-helix | 372-398 | 27 | |
| α-helix | 401-404 | 4 | |
| β-strand | 405 | 1 | 8 |
| α-helix | 407-409 | 3 | |
| α-helix | 416-439 | 24 | |
| α-helix | 441-443 | 3 | |
| α-helix | 444-460 | 17 | |
| α-helix | 462-475 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 384-409 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Endosomal/lysosomal potassium channel TMEM175 | A, B | protein | 504 | Homo sapiens | Q9BSA9 (AlphaFold model) |
| Lysosome-associated membrane glycoprotein 1 | C, D | protein | 417 | Homo sapiens | P11279 (AlphaFold model) |
>8FY5_1 Endosomal/lysosomal potassium channel TMEM175 (chains A, B) MSQPRTPEQALDTPGDCPPGRRDEDAGEGIQCSQRMLSFSDALLSIIATVMILPVTHTEI SPEQQFDRSVQRLLATRIAVYLMTFLIVTVAWAAHTRLFQVVGKTDDTLALLNLACMMTI TFLPYTFSLMVTFPDVPLGIFLFCVCVIAIGVVQALIVGYAFHFPHLLSPQIQRSAHRAL YRRHVLGIVLQGPALCFAAAIFSLFFVPLSYLLMVTVILLPYVSKVTGWCRDRLLGHREP SAHPVEVFSFDLHEPLSKERVEAFSDGVYAIVATLLILDICEDNVPDPKDVKERFSGSLV AALSATGPRFLAYFGSFATVGLLWFAHHSLFLHVRKATRAMGLLNTLSLAFVGGLPLAYQ QTSAFARQPRDELERVRVSCTIIFLASIFQLAMWTTALLHQAETLQPSVWFGGREHVLMF AKLALYPCASLLAFASTCLLSRFSVGIFHLMQIAVPCAFLLLRLLVGLALATLRVLRGLA RPEHPPPAPTGQDDPQSQLLPAPC
>8FY5_2 Lysosome-associated membrane glycoprotein 1 (chains C, D) MAAPGSARRPLLLLLLLLLLGLMHCASAAMFMVKNGNGTACIMANFSAAFSVNYDTKSGP KNMTFDLPSDATVVLNRSSCGKENTSDPSLVIAFGRGHTLTLNFTRNATRYSVQLMSFVY NLSDTHLFPNASSKEIKTVESITDIRADIDKKYRCVSGTQVHMNNVTVTLHDATIQAYLS NSSFSRGETRCEQDRPSPTTAPPAPPSPSPSPVPKSPSVDKYNVSGTNGTCLLASMGLQL NLTYERKDNTTVTRLLNINPNKTSASGSCGAHLVTLELHSEGTTVLLFQFGMNASSSRFF LQGIQLNTILPDARDPAFKAANGSLRALQATVGNSYKCNAEEHVRVTKAFSVNIFKVWVQ AFKVEGGQFGSVEECLLDENSMLIPIAVGGALAGLVLIVLIAYLVGRKRSHAGYQTI
Lysosomal LAMP proteins regulate lysosomal pH by direct inhibition of the TMEM175 channel. Zhang, J., Zeng, W., Han, Y. et al. Mol Cell (2023) 83:2524-2539.e7. DOI 10.1016/j.molcel.2023.06.004 · PubMed
Other PDB entries of the same protein (UniProt Q9BSA9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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