Structure of human glutamate dehydrogenase-apo form. Determined by X-ray diffraction at 2.7 Å resolution. Released 6 Mar 2002.
Explore 1L1F in 3D Show helices and sheets RCSB PDB PDBe
1L1F contains 138 α-helices and 120 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 | 13-37 | 25 | |
| α-helix | 38-40 | 3 | |
| α-helix | 42-44 | 3 | |
| α-helix | 46-49 | 4 | |
| α-helix | 51-56 | 6 | |
| β-strand | 61-70 | 10 | 1 |
| β-strand | 76-85 | 10 | 1 |
| β-strand | 93-96 | 4 | 2 |
| β-strand | 97-99 | 3 | 1 |
| α-helix | 105-121 | 17 | |
| β-strand | 127-128 | 2 | 2 |
| β-strand | 129-133 | 5 | 1 |
| α-helix | 137-139 | 3 | |
| α-helix | 142-158 | 17 | |
| β-strand | 167-170 | 4 | 2 |
| β-strand | 172 | 1 | 3 |
| β-strand | 175 | 1 | 3 |
| α-helix | 177-189 | 13 | |
| α-helix | 198-200 | 3 | |
| α-helix | 207-209 | 3 | |
| α-helix | 218-231 | 14 | |
| α-helix | 234-240 | 7 | |
| β-strand | 250-254 | 5 | 4 |
| α-helix | 258-269 | 12 | |
| β-strand | 273-277 | 5 | 4 |
| β-strand | 278 | 1 | 5 |
| β-strand | 283 | 1 | 5 |
| β-strand | 285 | 1 | 6 |
| α-helix | 292-301 | 10 | |
| β-strand | 312 | 1 | 6 |
| β-strand | 325-328 | 4 | 4 |
| β-strand | 335 | 1 | 7 |
| α-helix | 340-342 | 3 | |
| β-strand | 347-349 | 3 | 4 |
| β-strand | 356 | 1 | 7 |
| α-helix | 358-366 | 9 | |
| β-strand | 370-372 | 3 | 4 |
| α-helix | 374-377 | 4 | |
| α-helix | 380-394 | 15 | |
| α-helix | 403-422 | 20 | |
| α-helix | 438-445 | 8 | |
| α-helix | 449-474 | 26 | |
| α-helix | 481-498 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamate Dehydrogenase 1 | A, B, C, D, E, F | protein | 505 | Homo sapiens | P00367 (AlphaFold model) |
>1L1F_1 Glutamate Dehydrogenase 1 (chains A, B, C, D, E, F) SEAVADREDDPNFFKMVEGFFDRGASIVEDKLVEDLRTRESEEQKRNRVRGILRIIKPCN HVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCA VVDVPFGGAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREM SWIADTYASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSIL GMTPGFGDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKL QHGSILGFPKAKPYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEA DKIFLERNIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQES LERKFGKHGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLD LRTAAYVNAIEKVFKVYNEAGVTFT
The structure of apo human glutamate dehydrogenase details subunit communication and allostery. Smith, T.J., Schmidt, T., Fang, J. et al. J Mol Biol (2002) 318:765-777. DOI 10.1016/S0022-2836(02)00161-4 · 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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