3AL3: TopBP1 BRCT7/8-BACH1 peptide complex

Crystal Structure of TopBP1 BRCT7/8-BACH1 peptide complex. Determined by X-ray diffraction at 2.15 Å resolution. Released 1 Dec 2010.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,961
Mol. weight: 27.84 kDa
Released: 1 Dec 2010

Explore 3AL3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3AL3 contains 14 α-helices and 10 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: 13 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	1269-1273	5	1
α-helix	1277-1289	13
β-strand	1293-1294	2	1
β-strand	1306-1309	4	1
α-helix	1316-1323	8
β-strand	1327-1329	3	1
α-helix	1332-1340	9
α-helix	1347-1349	3
β-strand	1350	1	1
α-helix	1354-1357	4
α-helix	1365-1385	21
β-strand	1398-1402	5	2
α-helix	1408-1417	10
β-strand	1421-1422	2	2
α-helix	1428-1430	3
β-strand	1436-1439	4	2
α-helix	1453-1458	6
β-strand	1462-1465	4	2
α-helix	1467-1474	8
α-helix	1478-1480	3
α-helix	1481-1484	4
β-strand	1485	1	2
α-helix	1487-1489	3

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1133-1135	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA topoisomerase 2-binding protein 1	A	protein	235	Homo sapiens	Q92547 (AlphaFold model)
Peptide of Fanconi anemia group J protein	B	protein	10		Q9BX63 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3AL3_1 DNA topoisomerase 2-binding protein 1 (chains A)
GPLGSLKKQYIFQLSSLNPQERIDYCHLIEKLGGLVIEKQCFDPTCTHIVVGHPLRNEKY
LASVAAGKWVLHRSYLEACRTAGHFVQEEDYEWGSSSILDVLTGINVQQRRLALAAMRWR
KKIQQRQESGIVEGAFSGWKVILHVDQSREAGFKRLLQSGGAKVLPGHSVPLFKEATHLF
SDLNKLKPDDSGVNIAEAAAQNVYCLRTEYIADYLMQESPPHVENYCLPEAISFI

Sequence of entity 2 (B), FASTA

>3AL3_2 Peptide of Fanconi anemia group J protein (chains B)
SIYFTPELYD

Primary citation

Molecular basis of BACH1/FANCJ recognition by TopBP1 in DNA replication checkpoint control. Leung, C.C., Gong, Z., Chen, J. et al. J Biol Chem (2011) 286:4292-4301. DOI 10.1074/jbc.M110.189555 · PubMed

Other PDB entries of the same protein (UniProt Q92547 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3PD7 1.26 Å, Crystal Structure of the Sixth BRCT Domain of Human TopBP1
3JVE 1.34 Å, Crystal Structure of the Sixth BRCT Domain of TopBP1
9MAT 1.65 Å, TopBP1 BRCT 7-8 Domain
7CMZ 1.7 Å, Crystal Structure of BRCT7/8 in Complex with the APS Motif of PHF8
3UEN 1.9 Å, Crystal structure of TopBP1 BRCT4/5 domains
3AL2 2.0 Å, Crystal Structure of TopBP1 BRCT7/8
3OLC 2.4 Å, Crystal structure of the N-terminal region of TopBP1
9MAW 2.45 Å, Crystal structure of TOPBP1BRCT7-8 domain in complex with 1-Adamantaneacetic acid
2XNK 2.6 Å, Structure and function of the Rad9-binding region of the DNA damage checkpoint adaptor…
3UEO 2.6 Å, Crystal structure of TopBP1 BRCT4/5 domains in complex with a phospho-peptide
2XNH 2.8 Å, Structure and function of the Rad9-binding region of the DNA damage checkpoint adaptor…
6RML 2.81 Å, Crystal structure of TOPBP1 BRCT0,1,2 in complex with a 53BP1 phosphopeptide

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