9DUO: Human PELP1-WDR18 complex

Human PELP1-WDR18 complex. Determined by electron microscopy at 2.66 Å resolution. Released 30 Apr 2025.

Method: Electron microscopy
Resolution: 2.66 Å
Organism: Homo sapiens
Chains: 4
Atoms: 13,187
Mol. weight: 231.85 kDa
Released: 30 Apr 2025

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

Secondary structure: helices and β-sheets

9DUO contains 78 α-helices and 68 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, 32 β-strands

Element	Residues	Length	Sheet
β-strand	6-12	7	1
β-strand	20-24	5	1
β-strand	30-34	5	1
β-strand	35	1	2
β-strand	39-47	9	3
β-strand	51-56	6	3
β-strand	61-66	6	3
β-strand	71	1	2
α-helix	72-73	2
β-strand	77-78	2	3
β-strand	83-88	6	4
β-strand	94-99	6	4
β-strand	102-107	6	4
β-strand	113-117	5	4
β-strand	124-129	6	5
β-strand	135-140	6	5
β-strand	145-149	5	5
α-helix	150-155	6
β-strand	166-168	3	5
β-strand	175-180	6	6
β-strand	188-193	6	6
β-strand	197-202	6	6
β-strand	208-213	6	6
β-strand	218-223	6	7
β-strand	229-234	6	7
β-strand	239-243	5	7
β-strand	253-254	2	6
α-helix	261-263	3
β-strand	264-265	2	7
β-strand	272-277	6	8
β-strand	283-288	6	8
β-strand	292-297	6	8
β-strand	302-308	7	8
β-strand	313-320	8	1
α-helix	321-322	2
α-helix	323-326	4
α-helix	335-337	3
β-strand	357-359	3	9
α-helix	363-365	3
α-helix	372-389	18

Chain B: 5 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	6-12	7	10
β-strand	20-24	5	10
β-strand	30-34	5	10
β-strand	35	1	11
β-strand	39-47	9	12
β-strand	51-56	6	12
β-strand	61-66	6	12
β-strand	71	1	11
β-strand	76-78	3	12
β-strand	83-88	6	13
β-strand	94-99	6	13
β-strand	102-107	6	13
β-strand	113-117	5	13
β-strand	124-129	6	14
β-strand	135-140	6	14
β-strand	145-149	5	14
α-helix	150-154	5
β-strand	166-168	3	14
β-strand	175-180	6	15
β-strand	188-193	6	15
β-strand	197-202	6	15
β-strand	208-213	6	15
β-strand	218-223	6	16
β-strand	229-234	6	16
β-strand	239-243	5	16
β-strand	253-254	2	15
β-strand	264-265	2	16
β-strand	272-277	6	17
β-strand	283-288	6	17
β-strand	292-297	6	17
β-strand	302-308	7	17
β-strand	313-320	8	10
α-helix	321-322	2
α-helix	323-326	4
α-helix	335-337	3
β-strand	357-359	3	18
α-helix	372-389	18

Chain C: 32 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	30-41	12
α-helix	66-76	11
α-helix	89-99	11
α-helix	102-104	3
α-helix	105-117	13
α-helix	121-138	18
α-helix	145-162	18
α-helix	166-175	10
α-helix	177-185	9
α-helix	189-191	3
α-helix	192-205	14
α-helix	208-213	6
α-helix	214-223	10
α-helix	230-240	11
α-helix	243-245	3
α-helix	256-278	23
α-helix	307-327	21
β-strand	334-336	3	18
α-helix	338-350	13
α-helix	362-387	26
α-helix	388-394	7
α-helix	395-408	14
α-helix	420-422	3
α-helix	425-442	18
α-helix	443-445	3
α-helix	452-466	15
α-helix	468-469	2
α-helix	519-536	18
α-helix	542-558	17
α-helix	569-571	3
α-helix	573-588	16
α-helix	598-608	11
α-helix	614-631	18

Chain D: 33 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	30-42	13
α-helix	66-76	11
α-helix	88-98	11
α-helix	102-104	3
α-helix	105-118	14
α-helix	121-139	19
α-helix	145-162	18
α-helix	166-175	10
α-helix	177-185	9
α-helix	189-191	3
α-helix	192-205	14
α-helix	208-213	6
α-helix	214-222	9
α-helix	230-240	11
α-helix	243-245	3
α-helix	255-278	24
α-helix	306-327	22
β-strand	334-336	3	9
α-helix	338-349	12
α-helix	353-355	3
α-helix	362-387	26
α-helix	388-394	7
α-helix	395-408	14
α-helix	420-422	3
α-helix	425-442	18
α-helix	443-445	3
α-helix	453-465	13
α-helix	519-536	18
α-helix	537-539	3
α-helix	542-560	19
α-helix	569-571	3
α-helix	573-588	16
β-strand	591	1	19
β-strand	594	1	19
α-helix	598-608	11
α-helix	614-631	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
WD repeat-containing protein 18	A, B	protein	434	Homo sapiens	Q9BV38 (AlphaFold model)
Proline-, glutamic acid- and leucine-rich protein 1	C, D	protein	644	Homo sapiens	Q8IZL8 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9DUO_1 WD repeat-containing protein 18 (chains A, B)
SNMAAPMEVAVCTDSAAPMWSCIVWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQLG
KNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVAESIHLWEVSTGNLLVILS
RHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLCSVLQADPSRIPAPRHVWSHHALPITDL
HCGFGGPLARVATSSLDQTVKLWEVSSGELLLSVLFDVSIMAVTMDLAEHHMFCGGSEGS
IFQVDLFTWPGQRERSFHPEQDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDV
QSKQCIRTVALKGPVTNAAILLAPVSMLSSDFRPSLPLPHFNKHLLGAEHGDEPRHGGLT
LRLGLHQQGSEPSYLDRTEQLQAVLCSTMEKSVLGGQDQLRVRVTELEDEVRNLRKINRD
LFDFSTRFITRPAK

Sequence of entity 2 (C, D), FASTA

>9DUO_2 Proline-, glutamic acid- and leucine-rich protein 1 (chains C, D)
SNMAAAVLSGPSAGSAAGVPGGTGGLSAVSSGPRLRLLLLESVSGLLQPRTGSAVAPVHP
PNRSAPHLPGLMCLLRLHGSVGGAQNLSALGALVSLSNARLSSIKTRFEGLCLLSLLVGE
SPTELFQQHCVSWLRSIQQVLQTQDPPATMELAVAVLRDLLRYAAQLPALFRDISMNHLP
GLLTSLLGLRPECEQSALEGMKACMTYFPRACGSLKGKLASFFLSRVDALSPQLQQLACE
CYSRLPSLGAGFSQGLKHTESWEQELHSLLASLHTLLGALYEGAETAPVQNEGPGVEMLL
SSEDGDAHVLLQLRQRFSGLARCLGLMLSSEFGAPVSVPVQEILDFICRTLSVSSKNISL
HGDGPLRLLLLPSIHLEALDLLSALILACGSRLLRFGILIGRLLPQVLNSWSIGRDSLSP
GQERPYSTVRTKVYAILELWVQVCGASAGMLQGGASGEALLTHLLSDISPPADALKLRSP
RGSPDGSLQTGKPSAPKKLKLDVGEAMAPPSHRKGDSNANSDVCAAALRGLSRTILMCGP
LIKEETHRRLHDLVLPLVMGVQQGEVLGSSPYTSSRCRRELYCLLLALLLAPSPRCPPPL
ACALQAFSLGQREDSLEVSSFCSEALVTCAALTHPRVPPLQPMG

Primary citation

Molecular insights into the overall architecture of human rixosome. Huang, J., Tong, L. Nat Commun (2025) 16:3288-3288. DOI 10.1038/s41467-025-58732-3 · PubMed

Other PDB entries of the same protein (UniProt Q9BV38 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8FL3 2.53 Å, Human nuclear pre-60S ribosomal subunit (State I2)
8FL2 2.67 Å, Human nuclear pre-60S ribosomal subunit (State I1)
7UWF 2.7 Å, Human Rix1 sub-complex scaffold
8FL4 2.89 Å, Human nuclear pre-60S ribosomal subunit (State I3)
9DUM 3.56 Å, Human PELP1-WDR18-TEX10 complex

Browse structure collections

About this viewer

MolViewer shows 9DUO directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.