9RSX: RACK1

Name: PDB 9RSX: Structure of RACK1 bound to the C-terminus of SERBP1 and the RIH region of ZAK
Published: 2025-12-10
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ribosome

Structure of RACK1 bound to the C-terminus of SERBP1 and the RIH region of ZAK. Determined by electron microscopy at 2.91 Å resolution. Released 10 Dec 2025.

Method: Electron microscopy
Resolution: 2.91 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,733
Mol. weight: 198.18 kDa
Released: 10 Dec 2025

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

Secondary structure: helices and β-sheets

9RSX contains 3 α-helices and 29 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 N2: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	611-616	6

Chain N3: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	394-396	3

Chain RD: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	223-225	3	1

Chain Rg: 1 helix, 28 β-strands

Element	Residues	Length	Sheet
β-strand	2-11	10	2
β-strand	18-23	6	3
β-strand	31-35	5	3
β-strand	40-44	5	3
β-strand	54-59	6	3
β-strand	66-71	6	4
β-strand	77-82	6	4
β-strand	87-91	5	4
β-strand	96-101	6	4
β-strand	108-113	6	5
β-strand	120-124	5	5
β-strand	129-132	4	5
β-strand	138-142	5	5
β-strand	151-156	6	1
β-strand	164-169	6	1
β-strand	174-178	5	1
β-strand	183-189	7	1
β-strand	195-200	6	6
β-strand	206-211	6	6
β-strand	215-220	6	6
β-strand	226-231	6	6
β-strand	236-241	6	7
β-strand	247-252	6	7
β-strand	255-260	6	7
β-strand	265-270	6	7
α-helix	282-285	4
β-strand	286-291	6	2
β-strand	297-302	6	2
β-strand	307-315	9	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase kinase kinase 20	N2	protein	800	Homo sapiens	Q9NYL2 (AlphaFold model)
Plasminogen activator inhibitor 1 RNA-binding protein	N3	protein	408	Homo sapiens	Q8NC51 (AlphaFold model)
40S ribosomal protein S3	RD	protein	243	Homo sapiens	P23396 (AlphaFold model)
Receptor of activated protein C kinase 1	Rg	protein	317	Homo sapiens	P63244 (AlphaFold model)

Sequence of entity 1 (N2), FASTA

>9RSX_1 Mitogen-activated protein kinase kinase kinase 20 (chains N2)
MSSLGASFVQIKFDDLQFFENCGGGSFGSVYRAKWISQDKEVAVKKLLKIEKEAEILSVL
SHRNIIQFYGVILEPPNYGIVTEYASLGSLYDYINSNRSEEMDMDHIMTWATDVAKGMHY
LHMEAPVKVIHRDLKSRNVVIAADGVLKICDFGASRFHNHTTHMSLVGTFPWMAPEVIQS
LPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERLTIPSSCPRSFAELLH
QCWEADAKKRPSFKQIISILESMSNDTSLPDKCNSFLHNKAEWRCEIEATLERLKKLERD
LSFKEQELKERERRLKMWEQKLTEQSNTPLLPSFEIGAWTEDDVYCWVQQLVRKGDSSAE
MSVYASLFKENNITGKRLLLLEEEDLKDMGIVSKGHIIHFKSAIEKLTHDYINLFHFPPL
IKDSGGEPEENEEKIVNLELVFGFHLKPGTGPQDCKWKMYMEMDGDEIAITYIKDVTFNT
NLPDAEILKMTKPPFVMEKWIVGIAKSQTVECTVTYESDVRTPKSTKHVHSIQWSRTKPQ
DEVKAVQLAIQTLFTNSDGNPGSRSDSSADCQWLDTLRMRQIASNTSLQRSQSNPILGSP
FFSHFDGQDSYAAAVRRPQVPIKYQQITPVNQSRSSSPTQYGLTKNFSSLHLNSRDSGFS
SGNTDTSSERGRYSDRSRNKYGRGSISLNSSPRGRYSGKSQHSTPSRGRYPGKFYRVSQS
ALNPHQSPDFKRSPRDLHQPNTIPGMPLHPETDSRASEEDSKVSEGGWTKVEYRKKPHRP
SPAKTNKERARGDHRGWRNF

Sequence of entity 2 (N3), FASTA

>9RSX_2 Plasminogen activator inhibitor 1 RNA-binding protein (chains N3)
MPGHLQEGFGCVVTNRFDQLFDDESDPFEVLKAAENKKKEAGGGGVGGPGAKSAAQAAAQ
TNSNAAGKQLRKESQKDRKNPLPPSVGVVDKKEETQPPVALKKEGIRRVGRRPDQQLQGE
GKIIDRRPERRPPRERRFEKPLEEKGEGGEFSVDRPIIDRPIRGRGGLGRGRGGRGRGMG
RGDGFDSRGKREFDRHSGSDRSSFSHYSGLKHEDKRGGSGSHNWGTVKDELTESPKYIQK
QISYNYSDLDQSNVTEETPEGEEHHPVADTENKENEVEEVKEEGPKEMTLDEWKAIQNKD
RAKVEFNIRKPNEGADGQWKKGFVLHKSKSEEAHAEDSVMDHHFRKPANDITSQLEINFG
DLGRPGRGGRGGRGGRGRGGRPNRGSRTDKSSASAPDVDDPEAFPALA

Sequence of entity 3 (RD), FASTA

>9RSX_3 40S ribosomal protein S3 (chains RD)
MAVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLG
EKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACY
GVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQG
VLGIKVKIMLPWDPTGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPV
PTA

Sequence of entity 4 (Rg), FASTA

>9RSX_4 Receptor of activated protein C kinase 1 (chains Rg)
MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALR
GHSHFVSDVVISSDGQFALSGSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQI
VSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNSSNPIIVSCGWDKLVKVWNLA
NCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALC
FSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFA
GYTDNLVRVWQVTIGTR

Primary citation

ZAK activation at the collided ribosome. Huso, V.L., Niu, S., Catipovic, M.A. et al. Nature (2026) 649:1051-1060. DOI 10.1038/s41586-025-09772-8 · PubMed

Other PDB entries of the same protein (UniProt Q9NYL2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5X5O 1.87 Å, Crystal structure of ZAK in complex with compound D2829
6JUU 1.9 Å, Crystal structure of ZAK in complex with compound 6r
6JUT 2.1 Å, Crystal structure of ZAK in complex with compound 6k
7YAW 2.1 Å, Crystal structure of ZAK in complex with compound YH-180
5HES 2.14 Å, Human leucine zipper- and sterile alpha motif-containing kinase (ZAK, MLT, HCCS-4, MRK,…
9RPV 2.35 Å, Structure of the ZAK-bound human disome
7YAZ 2.54 Å, Crystal structure of ZAK in complex with compound YH-186

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