9F4P: UP1

UP1 in complex with Z1217960891. Determined by X-ray diffraction at 1.4 Å resolution. Released 8 May 2024.

Method: X-ray diffraction
Resolution: 1.4 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,570
Mol. weight: 22.57 kDa
Ligands: Q49
Released: 8 May 2024

Explore 9F4P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9F4P contains 9 α-helices and 12 β-strands across 1 chain. 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, 12 β-strands

Element	Residues	Length	Sheet
α-helix	8-10	3
α-helix	11-14	4
β-strand	15-19	5	1
α-helix	27-34	8
α-helix	35-37	3
β-strand	40-47	8	1
β-strand	54-62	9	1
α-helix	65-73	9
α-helix	75	1
α-helix	77	1
β-strand	78-79	2	2
β-strand	82-83	2	2
β-strand	85-88	4	1
β-strand	106-110	5	3
α-helix	118-125	8
β-strand	131-138	8	3
β-strand	145-153	9	3
α-helix	156-164	9
β-strand	169-170	2	4
β-strand	173-174	2	4
β-strand	176-179	4	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed	A	protein	198	Homo sapiens	P09651 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9F4P_1 Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed (chains A)
GPMGSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGF
GFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTE
EHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEV
RKALSKQEMASASSSQRG

Ligands and cofactors

ID	Name	Formula	Copies
Q49	(3S)-3-(3-fluorophenoxy)-1-methylpyrrolidin-2-one	C11 H12 F N O2	1

Primary citation

Enhanced identification of small molecules binding to hnRNPA1 via cryptic pockets mapping coupled with X-ray fragment screening. Dunnett, L., Das, S., Venditti, V. et al. J Biol Chem (2025) 301:108335-108335. DOI 10.1016/j.jbc.2025.108335 · PubMed

Other PDB entries of the same protein (UniProt P09651 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5ZGL 0.95 Å, hnRNP A1 segment GGGYGGS (residues 234-240)
6J60 0.96 Å, hnRNP A1 reversible amyloid core GFGGNDNFG (residues 209-217)
1L3K 1.1 Å, UP1, the two RNA-recognition motif domain of hnrnp A1
6BXX 1.1 Å, GYNGFG from low-complexity domain of hnRNPA1, residues 243-248
9F4G 1.4 Å, UP1 in complex with Z1373445602
9F4H 1.4 Å, UP1 in complex with Z106579662
9F4J 1.4 Å, UP1 in complex with Z416341642
9F4L 1.4 Å, UP1 in complex with Z104584152
9F4N 1.4 Å, UP1 in complex with Z137811222
9F4O 1.4 Å, UP1 in complex with Z991506900
9F4Q 1.4 Å, UP1 in complex with Z641239276
9F4S 1.4 Å, UP1 in complex with Z56880342

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