3G65: Cell cycle checkpoint control protein RAD9A

Name: PDB 3G65: Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex
Published: 2009-05-26
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: cell cycle

Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 26 May 2009.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 3
Atoms: 6,150
Mol. weight: 96.04 kDa
Released: 26 May 2009

Explore 3G65 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3G65 contains 27 α-helices and 53 β-strands across 3 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: 9 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	1
α-helix	8-21	14
β-strand	26-32	7	2
β-strand	35-41	7	2
β-strand	47-53	7	2
β-strand	73-76	4	2
α-helix	77-81	5
β-strand	96-101	6	1
β-strand	108-113	6	1
α-helix	115-117	3
β-strand	119-124	6	1
α-helix	138-140	3
β-strand	144-148	5	2
α-helix	149-155	7
β-strand	165-171	7	3
β-strand	175-180	6	3
α-helix	191-193	3
β-strand	194-199	6	3
α-helix	201-203	3
β-strand	206-208	3	2
β-strand	214-218	5	3
α-helix	219-231	13
β-strand	235-239	5	2
α-helix	246	1
β-strand	247-252	6	2
β-strand	257-262	6	2

Chain B: 8 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	17-21	5	4
α-helix	25-32	8
β-strand	39-44	6	5
β-strand	48-55	8	5
β-strand	59-66	8	5
β-strand	72-75	4	4
β-strand	80-85	6	5
α-helix	86-93	8
β-strand	107-111	5	4
α-helix	118	1
β-strand	119-125	7	4
β-strand	128-134	7	4
α-helix	135-136	2
β-strand	152-159	8	5
α-helix	160-168	9
β-strand	177-181	5	1
β-strand	188-193	6	1
β-strand	197-202	6	1
β-strand	210-215	6	5
β-strand	219-223	5	1
α-helix	225-227	3
α-helix	229-231	3
α-helix	232-235	4
β-strand	240-246	7	5
β-strand	251-258	8	5
β-strand	264-271	8	5

Chain C: 10 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	3
α-helix	10-26	17
β-strand	29-34	6	6
β-strand	38-44	7	6
β-strand	53-59	7	6
α-helix	60-62	3
β-strand	66-70	5	3
β-strand	79-84	6	6
α-helix	85-93	9
β-strand	100-106	7	3
β-strand	112-119	8	3
α-helix	126	1
β-strand	127-134	8	3
β-strand	137	1	6
α-helix	138-139	2
α-helix	140-146	7
α-helix	148-150	3
β-strand	156-159	4	6
α-helix	160	1
α-helix	163-174	12
β-strand	179-184	6	4
β-strand	190-195	6	4
β-strand	199-204	6	4
β-strand	228-233	6	4
α-helix	234-243	10
β-strand	251-256	6	6
β-strand	260-267	8	6
β-strand	270-276	7	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cell cycle checkpoint control protein RAD9A	A	protein	296	Homo sapiens	Q99638 (AlphaFold model)
Cell cycle checkpoint protein RAD1	B	protein	282	Homo sapiens	O60671 (AlphaFold model)
Checkpoint protein HUS1	C	protein	280	Homo sapiens	O60921 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3G65_1 Cell cycle checkpoint control protein RAD9A (chains A)
MKCLVTGGNVKVLGKAVHSLSRIGDELYLEPLEDGLSLRTVNSSRSAYACFLFAPLFFQQ
YQAATPGQDLLRCKILMKSFLSVFRSLAMLEKTVEKCCISLNGRSSRLVVQLHCKFGVRK
THNLSFQDCESLQAVFDPASCPHMLRAPARVLGEAVLPFSPALAEVTLGIGRGRRVILRS
YHEEEADSTAKAMVTEMCLGEEDFQQLQAQEGVAITFCLKEFRGLLSFAESANLNLSIHF
DAPGRPAIFTIKDSLLDGHFVLATLSDTDSGTTSTSLEVLFQGPLSGSGGHHHHHH

Sequence of entity 2 (B), FASTA

>3G65_2 Cell cycle checkpoint protein RAD1 (chains B)
MPLLTQQIQDEDDQYSLVASLDNVRNLSTILKAIHFREHATCFATKNGIKVTVENAKCVQ
ANAFIQAGIFQEFKVQEESVTFRINLTVLLDCLSIFGSSPMPGTLTALRMCYQGYGYPLM
LFLEEGGVVTVCKINTQEPEETLDFDFCSTNVINKIILQSEGLREAFSELDMTSEVLQIT
MSPDKPYFRLSTFGNAGSSHLDYPKDSDLMEAFHCNQTQVNRYKISLLKPSTKALVLSCK
VSIRTDNRGFLSLQYMIRNEDGQICFVEYYCCPDEEVPESES

Sequence of entity 3 (C), FASTA

>3G65_3 Checkpoint protein HUS1 (chains C)
MKFRAKIVDGACLNHFTRISNMIAKLAKTCTLRISPDKLNFILCDKLANGGVSMWCELEQ
ENFFNEFQMEGVSAENNEIYLELTSENLSRALKTAQNARALKIKLTNKHFPCLTVSVELL
SMSSSSRIVTHDIPIKVIPRKLWKDLQEPVVPDPDVSIYLPVLKTMKSVVEKMKNISNHL
VIEANLDGELNLKIETELVCVTTHFKDLGNPPLASESTHEDRNVEHMAEVHIDIRKLLQF
LAGQQVNPTKALCNIVNNKMVHFDLLHEDVSLQYFIPALS

Primary citation

Crystal structure of the rad9-rad1-hus1 DNA damage checkpoint complex--implications for clamp loading and regulation. Dore, A.S., Kilkenny, M.L., Rzechorzek, N.J. et al. Mol Cell (2009) 34:735-745. DOI 10.1016/j.molcel.2009.04.027 · PubMed

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

8JZY 1.5 Å, RPA70N-RAD9 fusion
8GNN 2.12 Å, Crystal structure of the human RAD9-RAD1-HUS1-RAD17 complex
6HM5 2.33 Å, Crystal structure of TOPBP1 BRCT0,1,2 in complex with a RAD9 phosphopeptide
6J8Y 2.4 Å, Crystal structure of the human RAD9-HUS1-RAD1-RHINO complex
3A1J 2.5 Å, Crystal structure of the human Rad9-Hus1-Rad1 complex
8WU8 2.81 Å, Crystal structure of the human RAD9-RAD1(F64A/M256A/F266A)-HUS1-RHINO(88-99) complex
3GGR 3.2 Å, Crystal Structure of the Human Rad9-Hus1-Rad1 complex
7Z6H 3.59 Å, Structure of DNA-bound human RAD17-RFC clamp loader and 9-1-1 checkpoint clamp

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