human liver mitochondrial Glutamate dehydrogenase 1. Determined by electron microscopy at 2.31 Å resolution. Released 21 Feb 2024.
Explore 8SK8 in 3D Show helices and sheets RCSB PDB PDBe
8SK8 contains 142 α-helices and 84 β-strands across 6 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 |
|---|---|---|---|
| α-helix | 65-69 | 5 | |
| α-helix | 70-87 | 18 | |
| α-helix | 95-109 | 15 | |
| β-strand | 114-123 | 10 | 1 |
| β-strand | 129-139 | 11 | 1 |
| β-strand | 146-152 | 7 | 1 |
| α-helix | 158-174 | 17 | |
| β-strand | 180-186 | 7 | 1 |
| α-helix | 190-192 | 3 | |
| α-helix | 195-211 | 17 | |
| β-strand | 220-223 | 4 | 1 |
| α-helix | 230-240 | 11 | |
| α-helix | 241-245 | 5 | |
| α-helix | 249-254 | 6 | |
| α-helix | 260-262 | 3 | |
| α-helix | 271-284 | 14 | |
| α-helix | 287-293 | 7 | |
| β-strand | 303-307 | 5 | 2 |
| α-helix | 311-322 | 12 | |
| β-strand | 326-331 | 6 | 2 |
| β-strand | 336-338 | 3 | 2 |
| α-helix | 345-355 | 11 | |
| β-strand | 365-366 | 2 | 2 |
| α-helix | 367 | 1 | |
| α-helix | 371-373 | 3 | |
| β-strand | 378-381 | 4 | 2 |
| β-strand | 388 | 1 | 3 |
| α-helix | 393-395 | 3 | |
| β-strand | 400-402 | 3 | 2 |
| β-strand | 409 | 1 | 3 |
| α-helix | 411-419 | 9 | |
| β-strand | 423-425 | 3 | 2 |
| α-helix | 427-430 | 4 | |
| α-helix | 433-447 | 15 | |
| α-helix | 456-478 | 23 | |
| α-helix | 491-498 | 8 | |
| α-helix | 502-527 | 26 | |
| α-helix | 534-551 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 65-69 | 5 | |
| α-helix | 70-87 | 18 | |
| α-helix | 95-109 | 15 | |
| β-strand | 114-123 | 10 | 4 |
| β-strand | 129-139 | 11 | 4 |
| β-strand | 146-152 | 7 | 4 |
| α-helix | 158-174 | 17 | |
| β-strand | 180-186 | 7 | 4 |
| α-helix | 190-192 | 3 | |
| α-helix | 195-211 | 17 | |
| β-strand | 220-223 | 4 | 4 |
| α-helix | 230-240 | 11 | |
| α-helix | 241-245 | 5 | |
| α-helix | 249-254 | 6 | |
| α-helix | 260-262 | 3 | |
| α-helix | 271-284 | 14 | |
| α-helix | 287-293 | 7 | |
| β-strand | 303-307 | 5 | 5 |
| α-helix | 311-322 | 12 | |
| β-strand | 326-331 | 6 | 5 |
| β-strand | 336-338 | 3 | 5 |
| α-helix | 345-355 | 11 | |
| β-strand | 365-366 | 2 | 5 |
| α-helix | 367 | 1 | |
| α-helix | 371-373 | 3 | |
| β-strand | 378-381 | 4 | 5 |
| β-strand | 388 | 1 | 6 |
| β-strand | 400-402 | 3 | 5 |
| β-strand | 409 | 1 | 6 |
| α-helix | 411-419 | 9 | |
| β-strand | 423-425 | 3 | 5 |
| α-helix | 427-430 | 4 | |
| α-helix | 433-447 | 15 | |
| α-helix | 456-478 | 23 | |
| α-helix | 491-498 | 8 | |
| α-helix | 502-527 | 26 | |
| α-helix | 534-551 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamate dehydrogenase 1, mitochondrial | A, B, C, D, E, F | protein | 558 | Homo sapiens | P00367 (AlphaFold model) |
>8SK8_1 Glutamate dehydrogenase 1, mitochondrial (chains A, B, C, D, E, F) MYRYLGEALLLSRAGPAALGSASADSAALLGWARGQPAAAPQPGLALAARRHYSEAVADR EDDPNFFKMVEGFFDRGASIVEDKLVEDLRTRESEEQKRNRVRGILRIIKPCNHVLSLSF PIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFG GAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTY ASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFG DKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILG FPKAKPYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLER NIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGK HGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYV NAIEKVFKVYNEAGVTFT
High-Resolution Structural Proteomics of Mitochondria Using the 'Build and Retrieve' Methodology. Zhang, Z., Tringides, M.L., Morgan, C.E. et al. Mol Cell Proteomics (2023) 22:100666-100666. DOI 10.1016/j.mcpro.2023.100666 · PubMed
Other PDB entries of the same protein (UniProt P00367 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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