6XLX: Cancer-associated G301D mutant of U2AF65

Crystal structure of cancer-associated G301D mutant of U2AF65 bound to AdML splice site. Determined by X-ray diffraction at 1.7 Å resolution. Released 7 Oct 2020.

Method: X-ray diffraction
Resolution: 1.7 Å
Organisms: Homo sapiens, synthetic construct
Chains: 2
Atoms: 1,862
Mol. weight: 24.74 kDa
Released: 7 Oct 2020

Explore 6XLX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6XLX contains 9 α-helices and 13 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, 13 β-strands

Element	Residues	Length	Sheet
α-helix	146-149	4
β-strand	150-154	5	1
α-helix	156-157	2
α-helix	162-175	14
β-strand	186-192	7	1
β-strand	197-202	6	1
α-helix	205-211	7
α-helix	212-214	3
β-strand	218-219	2	2
β-strand	222-223	2	2
β-strand	225-227	3	1
α-helix	234-235	2
β-strand	251	1	3
β-strand	261-264	4	3
α-helix	272-280	9
β-strand	285-292	8	3
β-strand	299-307	9	3
α-helix	312-320	9
β-strand	324-325	2	4
β-strand	328-329	2	4
β-strand	331-334	4	3
α-helix	335-338	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Splicing factor U2AF 65 kDa subunit	A	protein	204	Homo sapiens	P26368 (AlphaFold model)
Dna/rna (5'-r(pupup(ud)pupu)-d(p(bru))-r(pcpc)-3')	B	RNA	8	synthetic construct

Sequence of entity 1 (A), FASTA

>6XLX_1 Splicing factor U2AF 65 kDa subunit (chains A)
GPLGSQMTRQARRLYVGNIPFGITEEAMMDFFNAQMRLGGLTQAPGNPVLAVQINQDKNF
AFLEFRSVDETTQAMAFDGIIFQGQSLKIRRPHDYQPLPGMSENPSVYVPGVVSTVVPDS
AHKLFIGGLPNYLNDDQVKELLTSFGPLKAFNLVKDSATGLSKDYAFCEYVDINVTDQAI
AGLNGMQLGDKKLLVQRASVGAKN

Sequence of entity 2 (B), FASTA

>6XLX_2 DNA/RNA (5'-R(P*UP*UP*(UD)P*UP*U)-D(P*(BRU))-R(P*CP*C)-3') (chains B)
UUUUUUCC

Primary citation

Representative cancer-associated U2AF2 mutations alter RNA interactions and splicing. Maji, D., Glasser, E., Henderson, S. et al. J Biol Chem (2020) 295:17148-17157. DOI 10.1074/jbc.RA120.015339 · PubMed

Other PDB entries of the same protein (UniProt P26368 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5W0G 1.07 Å, Structure of U2AF65 (U2AF2) RRM1 at 1.07 resolution
5W0H 1.11 Å, Structure of U2AF65 (U2AF2) RRM2 at 1.11 Angstrom Resolution
6XLV 1.4 Å, Crystal structure of leukemia-associated N196K mutant of U2AF65 bound to AdML splice site
9C7A 1.4 Å, Crystal structure of R149W neurodevelopmental disease-associated U2AF2 variant
9C7B 1.4 Å, Crystal structure of R150H neurodevelopmental disease-associated U2AF2 variant
2HZC 1.47 Å, Crystal structure of the N-terminal RRM of the U2AF large subunit
7S3A 1.48 Å, Crystal structure of intact U2AF65 RRM-region bound to AdML-C5 oligonucleotide
5EV3 1.5 Å, Structure III of Intact U2AF65 Recognizing the 3' Splice Site Signal
6XLW 1.5 Å, Crystal structure of U2AF65 bound to AdML splice site sequence
7S3C 1.51 Å, Crystal structure of intact U2AF65 RRM-region bound to AdML-A5 oligonucleotide
5EV4 1.57 Å, Structure IV of Intact U2AF65 Recognizing the 3' Splice Site Signal
7SN6 1.8 Å, U2AF65 uhm bound to SF3B155 ULM5

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