8GNN: Human RAD9-RAD1-HUS1-RAD17 complex

Crystal structure of the human RAD9-RAD1-HUS1-RAD17 complex. Determined by X-ray diffraction at 2.12 Å resolution. Released 8 Mar 2023.

Method
X-ray diffraction
Resolution
2.12 Å
Organism
Homo sapiens
Chains
4
Atoms
6,546
Mol. weight
95.5 kDa
Released
8 Mar 2023

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

Secondary structure: helices and β-sheets

8GNN contains 32 α-helices and 56 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: 11 helices, 19 β-strands

ElementResiduesLengthSheet
β-strand2-651
α-helix9-2113
β-strand26-3272
β-strand35-4172
β-strand47-5372
α-helix55-573
β-strand60-6231
α-helix69-713
β-strand73-7642
α-helix77-837
α-helix87-937
β-strand94-10181
β-strand108-11471
α-helix115-1173
β-strand119-12461
β-strand127-12822
α-helix138-1403
β-strand143-14862
α-helix149-1568
β-strand165-17173
β-strand175-18063
α-helix191-1933
β-strand194-19963
α-helix201-2033
β-strand206-20832
β-strand214-21853
α-helix219-23113
β-strand235-24062
β-strand247-25262
β-strand256-26272
Chain B: 10 helices, 18 β-strands
ElementResiduesLengthSheet
β-strand2-763
α-helix10-2617
β-strand29-3464
β-strand38-4474
β-strand53-5974
α-helix60-623
β-strand66-7053
β-strand79-8464
α-helix85-9511
β-strand100-10783
β-strand111-11993
β-strand127-13483
β-strand136-13724
α-helix138-1392
α-helix140-1467
α-helix148-1503
β-strand156-15944
α-helix163-17412
β-strand179-18465
β-strand190-19565
β-strand199-20575
α-helix221-2233
α-helix226-2272
β-strand228-23365
α-helix234-2429
β-strand250-25674
β-strand260-26784
β-strand270-27784
Chain C: 10 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand17-2155
α-helix25-328
β-strand39-4466
β-strand48-5586
β-strand59-6686
α-helix67-693
β-strand72-7545
β-strand80-8566
α-helix86-938
β-strand107-11265
α-helix1181
β-strand119-12575
β-strand128-13475
β-strand13716
α-helix138-1436
α-helix149-1513
β-strand152-15986
α-helix161-1688
β-strand176-18161
β-strand188-19361
β-strand197-20371
β-strand210-21566
β-strand219-22461
α-helix225-2284
α-helix229-2313
α-helix232-2376
β-strand238-24696
β-strand251-25886
β-strand264-27186
Chain D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix17-193

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)
Cell cycle checkpoint protein RAD17Dprotein11Homo sapiensO75943 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8GNN_1 Cell cycle checkpoint control protein RAD9A (chains A)
MKCLVTGGNVKVLGKAVHSLSRIGDELYLEPLEDGLSLRTVNSSRSAYACFLFAPLFFQQ
YQAATPGQDLLRCKILMKSFLSVFRSLAMLEKTVEKCCISLNGRSSRLVVQLHCKFGVRK
THNLSFQDCESLQAVFDPASCPHMLRAPARVLGEAVLPFSPALAEVTLGIGRGRRVILRS
YHEEEADSTAKAMVTEMCLGEEDFQQLQAQEGVAITFCLKEFRGLLSFAESANLNLSIHF
DAPGRPAIFTIKDSLLDGHFVLATLSDTDS
Sequence of entity 2 (B), FASTA
>8GNN_2 Checkpoint protein HUS1 (chains B)
MHHHHHHKFRAKIVDGACLNHFTRISNMIAKLAKTCTLRISPDKLNFILCDKLANGGVSM
WCELEQENFFNEFQMEGVSAENNEIYLELTSENLSRALKTAQNARALKIKLTNKHFPCLT
VSVELLSMSSSSRIVTHDIPIKVIPRKLWKDLQEPVVPDPDVSIYLPVLKTMKSVVEKMK
NISNHLVIEANLDGELNLKIETELVCVTTHFKDLGNPPLASESTHEDRNVEHMAEVHIDI
RKLLQFLAGQQVNPTKALCNIVNNKMVHFDLLHEDVSLQYFIPALS
Sequence of entity 3 (C), FASTA
>8GNN_3 Cell cycle checkpoint protein RAD1 (chains C)
MPLLTQQIQDEDDQYSLVASLDNVRNLSTILKAIHFREHATCFATKNGIKVTVENAKCVQ
ANAFIQAGIFQEFKVQEESVTFRINLTVLLDCLSIFGSSPMPGTLTALRMCYQGYGYPLM
LFLEEGGVVTVCKINTQEPEETLDFDFCSTNVINKIILQSEGLREAFSELDMTSEVLQIT
MSPDKPYFRLSTFGNAGSSHLDYPKDSDLMEAFHCNQTQVNRYKISLLKPSTKALVLSCK
VSIRTDNRGFLSLQYMIRNEDGQICFVEYYCCPDEEVPESES
Sequence of entity 4 (D), FASTA
>8GNN_4 Cell cycle checkpoint protein RAD17 (chains D)
TDWVDPSFDDF

Primary citation

The 9-1-1 DNA clamp subunit RAD1 forms specific interactions with clamp loader RAD17, revealing functional implications for binding-protein RHINO. Hara, K., Hishiki, A., Hoshino, T. et al. J Biol Chem (2023) 299:103061-103061. DOI 10.1016/j.jbc.2023.103061 · PubMed

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

Browse structure collections

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