8HQ6: KL2

KL2 in complex with CRM1-Ran-RanBP1. Determined by X-ray diffraction at 2.03 Å resolution. Released 25 Oct 2023.

Method

X-ray diffraction

Resolution

2.03 Å

Organisms

Homo sapiens, Saccharomyces cerevisiae

Chains

3

Atoms

11,668

Mol. weight

158.86 kDa

Ligands

MG, GTP, GLU, MFF

Released

25 Oct 2023

Explore 8HQ6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8HQ6 contains 82 α-helices and 14 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: 14 helices, 7 β-strands

Molecules and chains

>8HQ6_1 GTP-binding nuclear protein Ran (chains A)
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK
FNVWDTAGLEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC
GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP
AAAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL

>8HQ6_2 YRB1 isoform 1 (chains B)
DIHFEPVVHLEKVDVKTMEEDEEVLYKVRAKLFRFDADAKEWKERGTGDCKFLKNKKTNK
VRILMRRDKTLKICANHIIAPEYTLKPNVGSDRSWVYACTADIAEGEAEAFTFAIRFGSK
ENADKFKEEFEKAQEINKKA

>8HQ6_3 CRM1 isoform 1 (chains C)
GGSMEGILDFSNDLDIALLDQVVSTFYQGEGVQQKQAQEILTKFQDNPDAWEKVDQILQF
STNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINK
SDLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQA
KALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILEL
LSTKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADL
KATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEERE
LFKTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEIQLYKSEREVLVYL
THLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSISGTMSEDTEKRFVVTVIKDL
LGLCEQKRGKDNKAVVARDIMYVVGEYPRFLKAHWNFLRTVILKLFEFMHETHEGVQDMA
CDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTADLQPQQVHTFYKACGIIISEE
RSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSETVKIIANIIKTNVAVCTSMGA
DFYPQLGHIYYNMLQLYRAVSSMISTQVAAEGLIATKTPKVRGLRTIKKEILKLVETYIS
KARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNCMTTVVEKVGHMIPQGVILILQ
SVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFLELPPAAFKLFVDAICWAFKH
NNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIFVSETFFVLTDSDHKSGFSKQ
ALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQYLANMLSNAFPHLTSEQIASFL
SALTKQCKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAEDKENA

Ligands and cofactors

Water and common crystallization additives (GOL, CL, NO3, DMS) are not listed.

Primary citation

Discovery of Aminoratjadone Derivatives as Potent Noncovalent CRM1 Inhibitors. Jian, L., Zscherp, R., Beutling, U. et al. J Med Chem (2023) 66:11940-11950. DOI 10.1021/acs.jmedchem.3c00549 · PubMed

Related structures

Other PDB entries of the same protein (UniProt P62826 (AlphaFold model), which also has an AlphaFold model), best resolution first:

• 3GJ0 1.48 Å, Crystal structure of human RanGDP
• 7MO5 1.55 Å, Crystal Structure of the ZnF4 of Nucleoporin NUP153 in complex with Ran-GDP
• 7MO1 1.6 Å, Crystal Structure of the ZnF1 of Nucleoporin NUP153 in complex with Ran-GDP
• 5CIQ 1.65 Å, Ran GDP wild type tetragonal crystal form
• 7MO2 1.65 Å, Crystal Structure of the ZnF2 of Nucleoporin NUP153 in complex with Ran-GDP
• 5CIT 1.75 Å, Ran GDP wild type monoclinic crystal form
• 5CIW 1.75 Å, Ran GDP Y39A mutant monoclinic crystal form
• 5CJ2 1.75 Å, Ran GDP Y39A mutant triclinic crystal form
• 1I2M 1.76 Å, Ran-RCC1-SO4 complex
• 4HAT 1.78 Å, Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1-Ran-RanBP1
• 3GJ3 1.79 Å, Crystal structure of human RanGDP-Nup153ZnF2 complex
• 3GJ5 1.79 Å, Crystal structure of human RanGDP-Nup153ZnF4 complex

Browse structure collections

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