4MZ6: Importin-alpha: dUTPase S11E NLS mutant complex

Structure of importin-alpha: dUTPase S11E NLS mutant complex. Determined by X-ray diffraction at 1.88 Å resolution. Released 13 Nov 2013.

Method: X-ray diffraction
Resolution: 1.88 Å
Organisms: Homo sapiens, Mus musculus
Chains: 3
Atoms: 3,721
Mol. weight: 57.97 kDa
Released: 13 Nov 2013

Explore 4MZ6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4MZ6 contains 34 α-helices and 0 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: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	16-18	3

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	16-19	4

Chain E: 32 helices, 0 β-strands

Element	Residues	Length
α-helix	78-85	8
α-helix	90-104	15
α-helix	112-117	6
α-helix	120-128	9
α-helix	134-148	15
α-helix	152-160	9
α-helix	163-170	8
α-helix	176-190	15
α-helix	194-202	9
α-helix	206-212	7
α-helix	218-220	3
α-helix	223-237	15
α-helix	243-245	3
α-helix	246-259	14
α-helix	265-278	14
α-helix	283-290	8
α-helix	295-302	8
α-helix	307-320	14
α-helix	325-333	9
α-helix	336-339	4
α-helix	340-343	4
α-helix	349-362	14
α-helix	367-375	9
α-helix	378-387	10
α-helix	391-407	17
α-helix	410-418	9
α-helix	422-427	6
α-helix	428-430	3
α-helix	434-454	21
α-helix	457-466	10
α-helix	469-476	8
α-helix	482-495	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial	A, C	protein	13	Homo sapiens	P33316 (AlphaFold model)
Importin subunit alpha-1	E	protein	509	Mus musculus	P52293 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>4MZ6_1 Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial (chains A, C)
AIEPSKRARPAEV

Sequence of entity 2 (E), FASTA

>4MZ6_2 Importin subunit alpha-1 (chains E)
MHHHHHHSSGLVPRGSGMLETAAALFERNHMDSPDLGTDDDDLAMADIGSNQGTVNWSVE
DIVKGINSNNLESQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGKTDCSPIQFE
SAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGDGSAFRDL
VIKHGAIDPLLALLAVPDLSTLACGYLRNLTWTLSNLCRNKNPAPPLDAVEQILPTLVRL
LHHNDPEVLADSCWAISYLTDGPNERIEMVVKKGVVPQLVKLLGATELPIVTPALRAIGN
IVTGTDEQTQKVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQIQQVVNHGLV
PFLVGVLSKADFKTQKEAAWAITNYTSGGTVEQIVYLVHCGIIEPLMNLLSAKDTKIIQV
ILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQRHENESVYKASLNLIEKYFSVE
EEEDQNVVPETTSEGFAFQVQDGAPGTFN

Primary citation

Phosphorylation adjacent to the nuclear localization signal of human dUTPase abolishes nuclear import: structural and mechanistic insights. Rona, G., Marfori, M., Borsos, M. et al. Acta Crystallogr D Biol Crystallogr (2013) 69:2495-2505. DOI 10.1107/S0907444913023354 · PubMed

Other PDB entries of the same protein (UniProt P33316 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3ARA 1.7 Å, Discovery of Novel Uracil Derivatives as Potent Human dUTPase Inhibitors
3ARN 1.8 Å, Human dUTPase in complex with novel uracil derivative
3EHW 1.8 Å, Human dUTPase in complex with alpha,beta-imido-dUTP and Mg2+: visualization of the…
5H4J 1.8 Å, Crystal structure of Human dUTPase in complex with N-[(1R)-1-[3-(Cyclopentyloxy)-phenyl]-…
7PWJ 1.94 Å, dUTPase from human in complex with Stl
1Q5H 2.0 Å, Human dUTP Pyrophosphatase complex with dUDP
1Q5U 2.0 Å, Human dutp pyrophosphatase
24OK 2.01 Å, Crystal structure of human dUTPase complexed with Zinc.
4MZ5 2.1 Å, Structure of importin-alpha: dUTPase NLS complex
2HQU 2.2 Å, Human dUTPase in complex with alpha,beta-iminodUTP and magnesium ion
8C8I 3.2 Å, Human dUTPase in complex with a potent proteinaceous inhibitor (Stl)

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