Crystal structure of the human 2-oxoadipate dehydrogenase DHTKD1 (E1). Determined by X-ray diffraction at 1.87 Å resolution. Released 24 Jun 2020.
Explore 6SY1 in 3D Show helices and sheets RCSB PDB PDBe
6SY1 contains 94 α-helices and 54 β-strands across 2 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 | 54-66 | 13 | |
| α-helix | 67-70 | 4 | |
| α-helix | 87-94 | 8 | |
| β-strand | 100-101 | 2 | 1 |
| β-strand | 112-113 | 2 | 1 |
| α-helix | 115-126 | 12 | |
| β-strand | 130-133 | 4 | 2 |
| α-helix | 140-155 | 16 | |
| α-helix | 160-183 | 24 | |
| α-helix | 198-212 | 15 | |
| β-strand | 216-220 | 5 | 2 |
| α-helix | 226-232 | 7 | |
| α-helix | 238-245 | 8 | |
| α-helix | 262-264 | 3 | |
| β-strand | 268-271 | 4 | 2 |
| β-strand | 279-283 | 5 | 2 |
| α-helix | 284-285 | 2 | |
| α-helix | 293-308 | 16 | |
| α-helix | 311-313 | 3 | |
| β-strand | 325-332 | 8 | 2 |
| α-helix | 333-338 | 6 | |
| α-helix | 341-348 | 8 | |
| β-strand | 359-365 | 7 | 2 |
| β-strand | 368-369 | 2 | 3 |
| β-strand | 372-373 | 2 | 3 |
| α-helix | 374-376 | 3 | |
| α-helix | 383-390 | 8 | |
| β-strand | 393-398 | 6 | 2 |
| α-helix | 402-419 | 18 | |
| β-strand | 423-428 | 6 | 2 |
| α-helix | 441-443 | 3 | |
| α-helix | 446-454 | 9 | |
| α-helix | 458-468 | 11 | |
| α-helix | 474-493 | 20 | |
| α-helix | 495-497 | 3 | |
| α-helix | 500-502 | 3 | |
| α-helix | 528-537 | 10 | |
| α-helix | 549-551 | 3 | |
| α-helix | 552-556 | 5 | |
| α-helix | 557-565 | 9 | |
| β-strand | 569 | 1 | 4 |
| α-helix | 571-584 | 14 | |
| β-strand | 588-593 | 6 | 5 |
| β-strand | 608-609 | 2 | 6 |
| β-strand | 616-617 | 2 | 6 |
| α-helix | 619-621 | 3 | |
| β-strand | 631-635 | 5 | 5 |
| α-helix | 641-653 | 13 | |
| β-strand | 657-662 | 6 | 5 |
| α-helix | 666-672 | 7 | |
| α-helix | 673-675 | 3 | |
| α-helix | 676-680 | 5 | |
| α-helix | 683-687 | 5 | |
| β-strand | 694-698 | 5 | 5 |
| α-helix | 713-719 | 7 | |
| β-strand | 735-737 | 3 | 5 |
| α-helix | 742-754 | 13 | |
| β-strand | 761-765 | 5 | 5 |
| α-helix | 768-770 | 3 | |
| β-strand | 777 | 1 | 4 |
| α-helix | 779-782 | 4 | |
| β-strand | 791-792 | 2 | 7 |
| α-helix | 799-801 | 3 | |
| β-strand | 804-808 | 5 | 7 |
| α-helix | 812-821 | 10 | |
| α-helix | 824-829 | 6 | |
| β-strand | 830-835 | 6 | 7 |
| β-strand | 837-839 | 3 | 5 |
| α-helix | 843-851 | 9 | |
| β-strand | 858-866 | 9 | 7 |
| α-helix | 872-883 | 12 | |
| β-strand | 888-892 | 5 | 7 |
| α-helix | 893-894 | 2 | |
| α-helix | 903-917 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 54-66 | 13 | |
| α-helix | 67-70 | 4 | |
| α-helix | 87-95 | 9 | |
| α-helix | 115-126 | 12 | |
| β-strand | 130-133 | 4 | 8 |
| α-helix | 140-155 | 16 | |
| α-helix | 156-159 | 4 | |
| α-helix | 160-183 | 24 | |
| α-helix | 198-211 | 14 | |
| β-strand | 216-220 | 5 | 8 |
| α-helix | 226-232 | 7 | |
| α-helix | 238-245 | 8 | |
| α-helix | 262-264 | 3 | |
| β-strand | 268-271 | 4 | 8 |
| α-helix | 277-278 | 2 | |
| β-strand | 279-283 | 5 | 8 |
| α-helix | 284-285 | 2 | |
| α-helix | 293-307 | 15 | |
| α-helix | 311-313 | 3 | |
| β-strand | 325-332 | 8 | 8 |
| α-helix | 333-338 | 6 | |
| α-helix | 341-347 | 7 | |
| β-strand | 359-365 | 7 | 8 |
| β-strand | 368-369 | 2 | 9 |
| β-strand | 372-373 | 2 | 9 |
| α-helix | 374-376 | 3 | |
| α-helix | 383-390 | 8 | |
| β-strand | 393-398 | 6 | 8 |
| α-helix | 402-419 | 18 | |
| β-strand | 423-428 | 6 | 8 |
| α-helix | 441-443 | 3 | |
| α-helix | 446-454 | 9 | |
| α-helix | 458-468 | 11 | |
| α-helix | 474-493 | 20 | |
| α-helix | 494-496 | 3 | |
| α-helix | 519-520 | 2 | |
| α-helix | 528-537 | 10 | |
| α-helix | 549-551 | 3 | |
| α-helix | 552-556 | 5 | |
| α-helix | 557-565 | 9 | |
| β-strand | 569 | 1 | 10 |
| α-helix | 571-584 | 14 | |
| β-strand | 588-593 | 6 | 11 |
| β-strand | 608-609 | 2 | 12 |
| β-strand | 616-617 | 2 | 12 |
| α-helix | 619-622 | 4 | |
| β-strand | 631-635 | 5 | 11 |
| α-helix | 641-651 | 11 | |
| β-strand | 657-662 | 6 | 11 |
| α-helix | 666-672 | 7 | |
| α-helix | 673-675 | 3 | |
| α-helix | 676-680 | 5 | |
| α-helix | 683-687 | 5 | |
| β-strand | 694-698 | 5 | 11 |
| α-helix | 713-719 | 7 | |
| β-strand | 735-737 | 3 | 11 |
| α-helix | 742-754 | 13 | |
| β-strand | 761-765 | 5 | 11 |
| α-helix | 768-770 | 3 | |
| β-strand | 777 | 1 | 10 |
| α-helix | 779-782 | 4 | |
| β-strand | 791-792 | 2 | 13 |
| α-helix | 799-801 | 3 | |
| β-strand | 804-808 | 5 | 13 |
| α-helix | 812-821 | 10 | |
| α-helix | 824-829 | 6 | |
| β-strand | 830-835 | 6 | 13 |
| β-strand | 837-839 | 3 | 11 |
| α-helix | 843-851 | 9 | |
| β-strand | 858-866 | 9 | 13 |
| α-helix | 872-883 | 12 | |
| β-strand | 888-892 | 5 | 13 |
| α-helix | 893-894 | 2 | |
| α-helix | 903-917 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial | A, B | protein | 898 | Homo sapiens | Q96HY7 (AlphaFold model) |
>6SY1_1 Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial (chains A, B) MHHHHHHSSGVDLGTENLYFQSMGALERPPVDHGLARLVTVYCEHGHKAAKINPLFTGQA LLENVPEIQALVQTLQGPFHTAGLLNMGKEEASLEEVLVYLNQIYCGQISIETSQLQSQD EKDWFAKRFEELQKETFTTEERKHLSKLMLESQEFDHFLATKFSTVKRYGGEGAESMMGF FHELLKMSAYSGITDVIIGMPHRGRLNLLTGLLQFPPELMFRKMRGLSEFPENFSATGDV LSHLTSSVDLYFGAHHPLHVTMLPNPSHLEAVNPVAVGKTRGRQQSRQDGDYSPDNSAQP GDRVICLQVHGDASFCGQGIVPETFTLSNLPHFRIGGSVHLIVNNQLGYTTPAERGRSSL YCSDIGKLVGCAIIHVNGDSPEEVVRATRLAFEYQRQFRKDVIIDLLCYRQWGHNELDEP FYTNPIMYKIIRARKSIPDTYAEHLIAGGLMTQEEVSEIKSSYYAKLNDHLNNMAHYRPP ALNLQAHWQGLAQPEAQITTWSTGVPLDLLRFVGMKSVEVPRELQMHSHLLKTHVQSRME KMMDGIKLDWATAEALALGSLLAQGFNVRLSGQDVGRGTFSQRHAIVVCQETDDTYIPLN HMDPNQKGFLEVSNSPLSEEAVLGFEYGMSIESPKLLPLWEAQFGDFFNGAQIIFDTFIS GGEAKWLLQSGIVILLPHGYDGAGPDHSSCRIERFLQMCDSAEEGVDGDTVNMFVVHPTT PAQYFHLLRRQMVRNFRKPLIVASPKMLLRLPAAVSTLQEMAPGTTFNPVIGDSSVDPKK VKTLVFCSGKHFYSLVKQRESLGAKKHDFAIIRVEELCPFPLDSLQQEMSKYKHVKDHIW SQEEPQNMGPWSFVSPRFEKQLACKLRLVGRPPLPVPAVGIGTVHLHQHEDILAKTFA
Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine catabolism. Bezerra, G.A., Foster, W.R., Bailey, H.J. et al. IUCrJ (2020) 7:693-706. DOI 10.1107/S205225252000696X · PubMed
Other PDB entries of the same protein (UniProt Q96HY7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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