6AJK: TFB1M and h45 in homo sapiens

Crystal structure of TFB1M and h45 in homo sapiens. Determined by X-ray diffraction at 3.0 Å resolution. Released 5 Jun 2019.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,944
Mol. weight: 45.79 kDa
Released: 5 Jun 2019

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

Secondary structure: helices and β-sheets

6AJK contains 18 α-helices and 9 β-strands across 1 chain. 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: 18 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	37	1	1
α-helix	41-49	9
β-strand	58-61	4	2
α-helix	68-74	7
β-strand	80-85	6	2
α-helix	88-90	3
α-helix	91-100	10
β-strand	105-109	5	2
α-helix	117-119	3
α-helix	123-125	3
β-strand	136-140	5	2
α-helix	144-160	17
α-helix	163-165	3
β-strand	171-177	7	2
α-helix	178-185	8
α-helix	186-187	2
α-helix	195-201	7
β-strand	204-212	9	2
α-helix	214-216	3
β-strand	218	1	1
β-strand	225-232	8	2
α-helix	242-252	11
α-helix	261-264	4
α-helix	265-267	3
α-helix	270-284	15
α-helix	292-294	3
α-helix	297-313	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Dimethyladenosine transferase 1, mitochondrial	A	protein	320	Homo sapiens	Q8WVM0 (AlphaFold model)
RNA (28-mer)	B	RNA	28	Homo sapiens

Sequence of entity 1 (A), FASTA

>6AJK_1 Dimethyladenosine transferase 1, mitochondrial (chains A)
MQAAKQLSQNFLLDLRLTDKIVRKAGNLTNAYVYEVGPGPGGITRSILNADVAELLVVEK
DTRFIPGLQMLSDAAPGKLRIVHGDVLTFKVEKAFSESLKRPWEDDPPNVHIIGNLPFSV
STPLIIKWLENISCRDGPFVYGRTQMTLTFQKEVAERLAANTGSKQRSRLSVMAQYLCNV
RHIFTIPGQAFVPKPEVDVGVVHFTPLIQPKIEQPFKLVEKVVQNVFQFRRKYCHRGLRM
LFPEAQRLESTGRLLELADIDPTLRPRQLSISHFKSLCDVYRKMCDEDPQLFAYNFREEL
KRRKSKNEEKEEDDAENYRL

Sequence of entity 2 (B), FASTA

>6AJK_2 RNA (28-MER) (chains B)
GGUAAGUGUACUGGAAAGUGCACUUGCC

Primary citation

Structural insights into dimethylation of 12S rRNA by TFB1M: indispensable role in translation of mitochondrial genes and mitochondrial function. Liu, X., Shen, S., Wu, P. et al. Nucleic Acids Res (2019) 47:7648-7665. DOI 10.1093/nar/gkz505 · PubMed

Other PDB entries of the same protein (UniProt Q8WVM0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8CSQ 2.54 Å, Human mitochondrial small subunit assembly intermediate (State B)
8CSR 2.54 Å, Human mitochondrial small subunit assembly intermediate (State C)
8CSP 2.66 Å, Human mitochondrial small subunit assembly intermediate (State A)
6AAX 2.99 Å, Crystal structure of TFB1M and h45 with SAM in homo sapiens
8CSU 3.03 Å, Human mitochondrial small subunit assembly intermediate (State C*)
9G5B 3.2 Å, Assembly intermediate of human mitochondrial ribosome small subunit (State A)
9H55 3.4 Å, Assembly intermediate of human mitochondrial ribosome small subunit in complex with NOA1…
9H52 3.9 Å, Assembly intermediate of human mitochondrial ribosome small subunit in complex with…

Browse structure collections

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