6SY1: Human 2-oxoadipate dehydrogenase DHTKD1

Crystal structure of the human 2-oxoadipate dehydrogenase DHTKD1 (E1). Determined by X-ray diffraction at 1.87 Å resolution. Released 24 Jun 2020.

Method
X-ray diffraction
Resolution
1.87 Å
Organism
Homo sapiens
Chains
2
Atoms
14,452
Mol. weight
202.78 kDa
Ligands
MG, TPP
Released
24 Jun 2020

Explore 6SY1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 46 helices, 28 β-strands

ElementResiduesLengthSheet
α-helix54-6613
α-helix67-704
α-helix87-948
β-strand100-10121
β-strand112-11321
α-helix115-12612
β-strand130-13342
α-helix140-15516
α-helix160-18324
α-helix198-21215
β-strand216-22052
α-helix226-2327
α-helix238-2458
α-helix262-2643
β-strand268-27142
β-strand279-28352
α-helix284-2852
α-helix293-30816
α-helix311-3133
β-strand325-33282
α-helix333-3386
α-helix341-3488
β-strand359-36572
β-strand368-36923
β-strand372-37323
α-helix374-3763
α-helix383-3908
β-strand393-39862
α-helix402-41918
β-strand423-42862
α-helix441-4433
α-helix446-4549
α-helix458-46811
α-helix474-49320
α-helix495-4973
α-helix500-5023
α-helix528-53710
α-helix549-5513
α-helix552-5565
α-helix557-5659
β-strand56914
α-helix571-58414
β-strand588-59365
β-strand608-60926
β-strand616-61726
α-helix619-6213
β-strand631-63555
α-helix641-65313
β-strand657-66265
α-helix666-6727
α-helix673-6753
α-helix676-6805
α-helix683-6875
β-strand694-69855
α-helix713-7197
β-strand735-73735
α-helix742-75413
β-strand761-76555
α-helix768-7703
β-strand77714
α-helix779-7824
β-strand791-79227
α-helix799-8013
β-strand804-80857
α-helix812-82110
α-helix824-8296
β-strand830-83567
β-strand837-83935
α-helix843-8519
β-strand858-86697
α-helix872-88312
β-strand888-89257
α-helix893-8942
α-helix903-91715
Chain B: 48 helices, 26 β-strands
ElementResiduesLengthSheet
α-helix54-6613
α-helix67-704
α-helix87-959
α-helix115-12612
β-strand130-13348
α-helix140-15516
α-helix156-1594
α-helix160-18324
α-helix198-21114
β-strand216-22058
α-helix226-2327
α-helix238-2458
α-helix262-2643
β-strand268-27148
α-helix277-2782
β-strand279-28358
α-helix284-2852
α-helix293-30715
α-helix311-3133
β-strand325-33288
α-helix333-3386
α-helix341-3477
β-strand359-36578
β-strand368-36929
β-strand372-37329
α-helix374-3763
α-helix383-3908
β-strand393-39868
α-helix402-41918
β-strand423-42868
α-helix441-4433
α-helix446-4549
α-helix458-46811
α-helix474-49320
α-helix494-4963
α-helix519-5202
α-helix528-53710
α-helix549-5513
α-helix552-5565
α-helix557-5659
β-strand569110
α-helix571-58414
β-strand588-593611
β-strand608-609212
β-strand616-617212
α-helix619-6224
β-strand631-635511
α-helix641-65111
β-strand657-662611
α-helix666-6727
α-helix673-6753
α-helix676-6805
α-helix683-6875
β-strand694-698511
α-helix713-7197
β-strand735-737311
α-helix742-75413
β-strand761-765511
α-helix768-7703
β-strand777110
α-helix779-7824
β-strand791-792213
α-helix799-8013
β-strand804-808513
α-helix812-82110
α-helix824-8296
β-strand830-835613
β-strand837-839311
α-helix843-8519
β-strand858-866913
α-helix872-88312
β-strand888-892513
α-helix893-8942
α-helix903-91715

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrialA, Bprotein898Homo sapiensQ96HY7 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>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

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg3
TPPThiamine diphosphateC12 H19 N4 O7 P2 S2

Primary citation

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:

Browse structure collections

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