9GR9: Homodimer of BACH1 BTB domain

Homodimer of BACH1 BTB domain. Determined by X-ray diffraction at 2.25 Å resolution. Released 11 Dec 2024.

Method: X-ray diffraction
Resolution: 2.25 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,788
Mol. weight: 56.23 kDa
Released: 11 Dec 2024

Explore 9GR9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9GR9 contains 23 α-helices and 24 β-strands across 4 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: 6 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	1
α-helix	16-29	14
β-strand	36-40	5	2
β-strand	43-47	5	2
α-helix	49-55	7
β-strand	56	1	3
α-helix	57-63	7
β-strand	71-75	5	2
α-helix	81-93	13
β-strand	95-99	5	4
α-helix	103-113	11
β-strand	115	1	3
α-helix	120-126	7

Chain B: 6 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	4
α-helix	16-29	14
β-strand	36-40	5	5
β-strand	43-47	5	5
α-helix	49-55	7
β-strand	56	1	6
α-helix	57-63	7
β-strand	71-74	4	5
α-helix	81-93	13
β-strand	95-99	5	1
α-helix	103-113	11
β-strand	115	1	6
α-helix	120-122	3

Chain C: 6 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	16-29	14
β-strand	36-40	5	7
β-strand	43-47	5	7
α-helix	49-55	7
β-strand	56	1	8
α-helix	57-63	7
β-strand	71-74	4	7
α-helix	81-93	13
α-helix	103-113	11
β-strand	115	1	8
α-helix	120-126	7

Chain D: 5 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	16-29	14
β-strand	36-40	5	9
β-strand	43-47	5	9
α-helix	49-55	7
β-strand	56	1	10
α-helix	57-63	7
β-strand	72-74	3	9
α-helix	81-93	13
α-helix	103-113	11
β-strand	115	1	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcription regulator protein BACH1	A, B, C, D	protein	124	Homo sapiens	O14867 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>9GR9_1 Transcription regulator protein BACH1 (chains A, B, C, D)
SMSVFAYESSVHSTNVLLSLNDQRKKDVLCDVTIFVEGQRFRAHRSVLAACSSYFHSRIV
GQADGELNITLPEEVTVKGFEPLIQFAYTAKLILSKENVDEVCKCVEFLSVHNIEESCFQ
FLKF

Primary citation

Dual BACH1 regulation by complementary SCF-type E3 ligases. Goretzki, B., Khoshouei, M., Schroder, M. et al. Cell (2024) 187:7585-7602.e25. DOI 10.1016/j.cell.2024.11.006 · PubMed

Other PDB entries of the same protein (UniProt O14867 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9GRA 1.47 Å, Homodimer of BACH1 BTB domain in complex with 2-Methyl-2,4-pentanediol
9GP5 1.9 Å, Homodimer of BACH1 F9A mutant BTB domain
2IHC 2.44 Å, Crystal structure of the bric-a-brac (BTB) domain of human BACH1
8UBT 3.1 Å, Structure of SCF-FBXL17-BACH1BTB E3 ligase complex
8S7D 3.2 Å, Cryo-EM structure of SKP1-FBXO22 in complex with a BACH1 BTB dimer at 3.2A resolution
8UAH 3.3 Å, Structure of BACH1 BTB domain-bound FBXL17 ubiquitin ligase
8UA3 3.8 Å, Cryo-EM Structure of FBOX22-BACH1BTB
8UA6 3.9 Å, Cryo-EM Structure of SCF-FBOX22-BACH1BTB
8UBV 4.1 Å, Cryo-EM structure of dimeric FBXL17-BACH1BTB E3 ubiquitin ligase complex
29HH 4.2 Å, Cryo-EM structure of the CUL1-RBX1-SKP1-FBXO22 SCF ubiquition ligase in complex with…
8UBU 4.6 Å, Cryo-EM structure of dimeric SCF-FBXL17-BACH1BTB E3 ligase complex close conformation

Browse structure collections

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