8WU8: Cell cycle checkpoint control protein RAD9A

Crystal structure of the human RAD9-RAD1(F64A/M256A/F266A)-HUS1-RHINO(88-99) complex. Determined by X-ray diffraction at 2.81 Å resolution. Released 14 Feb 2024.

Method
X-ray diffraction
Resolution
2.81 Å
Organism
Homo sapiens
Chains
4
Atoms
6,171
Mol. weight
95.34 kDa
Released
14 Feb 2024

Explore 8WU8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8WU8 contains 25 α-helices and 58 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: 8 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand2-651
α-helix9-2113
β-strand26-2722
β-strand28-3253
β-strand35-4173
β-strand47-5373
α-helix55-573
β-strand60-6231
β-strand75-7622
α-helix77-848
α-helix88-925
β-strand96-10051
β-strand108-11361
α-helix115-1173
β-strand119-12461
β-strand13414
α-helix138-1403
β-strand143-14863
α-helix149-1557
β-strand165-17175
β-strand175-18065
β-strand194-19965
β-strand206-20833
β-strand214-21855
α-helix219-23113
β-strand235-24063
β-strand247-25263
β-strand256-26273
Chain B: 7 helices, 18 β-strands
ElementResiduesLengthSheet
β-strand2-765
α-helix10-2617
β-strand29-3466
β-strand38-4366
β-strand53-5976
α-helix60-623
β-strand66-7055
β-strand79-8466
α-helix85-939
β-strand100-10785
β-strand111-11995
β-strand127-13485
β-strand13716
α-helix140-1434
α-helix144-1463
β-strand156-15946
α-helix163-17412
β-strand179-18577
β-strand190-19567
β-strand199-20577
β-strand227-23377
α-helix234-2418
β-strand250-25676
β-strand260-26676
β-strand270-27786
Chain C: 9 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand17-2157
α-helix25-328
β-strand39-4578
β-strand48-5588
β-strand59-6578
β-strand72-7547
β-strand80-8568
α-helix86-938
β-strand107-11267
α-helix1181
β-strand119-12577
β-strand128-13477
β-strand13718
α-helix138-1403
α-helix142-1454
β-strand152-15988
α-helix160-1689
β-strand176-18161
β-strand187-19481
β-strand197-20371
β-strand210-21568
β-strand219-22461
α-helix225-2284
α-helix229-2313
α-helix232-2354
β-strand240-24678
β-strand251-25888
β-strand264-27188
Chain D: 1 helix, 1 β-strand
ElementResiduesLengthSheet
α-helix91-944
β-strand9614

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cell cycle checkpoint control protein RAD9AAprotein270Homo sapiensQ99638 (AlphaFold model)
Checkpoint protein HUS1Bprotein286Homo sapiensO60921 (AlphaFold model)
Cell cycle checkpoint protein RAD1Cprotein282Homo sapiensO60671 (AlphaFold model)
RAD9, HUS1, RAD1-interacting nuclear orphan protein 1Dprotein12Homo sapiensQ9BSD3 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8WU8_1 Cell cycle checkpoint control protein RAD9A (chains A)
MKCLVTGGNVKVLGKAVHSLSRIGDELYLEPLEDGLSLRTVNSSRSAYACFLFAPLFFQQ
YQAATPGQDLLRCKILMKSFLSVFRSLAMLEKTVEKCCISLNGRSSRLVVQLHCKFGVRK
THNLSFQDCESLQAVFDPASCPHMLRAPARVLGEAVLPFSPALAEVTLGIGRGRRVILRS
YHEEEADSTAKAMVTEMCLGEEDFQQLQAQEGVAITFCLKEFRGLLSFAESANLNLSIHF
DAPGRPAIFTIKDSLLDGHFVLATLSDTDS
Sequence of entity 2 (B), FASTA
>8WU8_2 Checkpoint protein HUS1 (chains B)
MHHHHHHKFRAKIVDGACLNHFTRISNMIAKLAKTCTLRISPDKLNFILCDKLANGGVSM
WCELEQENFFNEFQMEGVSAENNEIYLELTSENLSRALKTAQNARALKIKLTNKHFPCLT
VSVELLSMSSSSRIVTHDIPIKVIPRKLWKDLQEPVVPDPDVSIYLPVLKTMKSVVEKMK
NISNHLVIEANLDGELNLKIETELVCVTTHFKDLGNPPLASESTHEDRNVEHMAEVHIDI
RKLLQFLAGQQVNPTKALCNIVNNKMVHFDLLHEDVSLQYFIPALS
Sequence of entity 3 (C), FASTA
>8WU8_3 Cell cycle checkpoint protein RAD1 (chains C)
MPLLTQQIQDEDDQYSLVASLDNVRNLSTILKAIHFREHATCFATKNGIKVTVENAKCVQ
ANAAIQAGIFQEFKVQEESVTFRINLTVLLDCLSIFGSSPMPGTLTALRMCYQGYGYPLM
LFLEEGGVVTVCKINTQEPEETLDFDFCSTNVINKIILQSEGLREAFSELDMTSEVLQIT
MSPDKPYFRLSTFGNAGSSHLDYPKDSDLMEAFHCNQTQVNRYKISLLKPSTKALVLSCK
VSIRTDNRGFLSLQYAIRNEDGQICAVEYYCCPDEEVPESES
Sequence of entity 4 (D), FASTA
>8WU8_4 RAD9, HUS1, RAD1-interacting nuclear orphan protein 1 (chains D)
TSKFPHLTFESP

Primary citation

Structural basis for intra- and intermolecular interactions on RAD9 subunit of 9-1-1 checkpoint clamp implies functional 9-1-1 regulation by RHINO. Hara, K., Tatsukawa, K., Nagata, K. et al. J Biol Chem (2024) 300:105751-105751. DOI 10.1016/j.jbc.2024.105751 · PubMed

Other PDB entries of the same protein (UniProt Q99638 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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