1W9C: CRM1 protein

Proteolytic fragment of CRM1 spanning six C-terminal HEAT repeats. Determined by X-ray diffraction at 2.3 Å resolution. Released 3 Dec 2004.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 5,300
Mol. weight: 72.54 kDa
Released: 3 Dec 2004

Explore 1W9C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1W9C contains 41 α-helices and 0 β-strands across 2 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: 21 helices, 0 β-strands

Element	Residues	Length
α-helix	711-713	3
α-helix	714-735	22
α-helix	738-741	4
α-helix	743-763	21
α-helix	769-775	7
α-helix	777-789	13
α-helix	793-795	3
α-helix	799-811	13
α-helix	812-818	7
α-helix	819-834	16
α-helix	842-858	17
α-helix	862-865	4
α-helix	868-881	14
α-helix	887-906	20
α-helix	908-914	7
α-helix	915-919	5
α-helix	920-931	12
α-helix	939-954	16
α-helix	970-985	16
α-helix	991-1003	13
α-helix	1008-1023	16

Chain B: 20 helices, 0 β-strands

Element	Residues	Length
α-helix	714-735	22
α-helix	737-741	5
α-helix	743-764	22
α-helix	769-775	7
α-helix	777-789	13
α-helix	793-795	3
α-helix	798-811	14
α-helix	812-818	7
α-helix	819-834	16
α-helix	842-858	17
α-helix	862-865	4
α-helix	868-882	15
α-helix	887-905	19
α-helix	908-914	7
α-helix	915-919	5
α-helix	920-931	12
α-helix	939-954	16
α-helix	970-985	16
α-helix	991-1003	13
α-helix	1008-1023	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
CRM1 protein	A, B	protein	321	HOMO SAPIENS	O14980 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1W9C_1 CRM1 PROTEIN (chains A, B)
VIQLGRIYLDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRS
NDPQMVAENFVPPLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAV
FECTLNMINKDFEEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTM
RNVADTGLQILFTLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASIL
AYMFNLVEEGKISTSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQ
DIPAFKEHLRDFLVQIKEFAG

Primary citation

Architecture of Crm1-Exportin 1 Suggests How Cooperativity is Achieved During Formation of a Nuclear Export Complex. Petosa, C., Schoehn, G., Askjaer, P. et al. Mol Cell (2004) 16:761. DOI 10.1016/J.MOLCEL.2004.11.018 · PubMed

Other PDB entries of the same protein (UniProt O14980 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9OGD 2.49 Å, Cryo-EM structure of human exportin-1 conjugated with selinexor and bound to human…
7B51 2.58 Å, Crystal structure of human CRM1 covalently modified by 2-mercaptoethanol at Cys528
9HFL 2.62 Å, Cryo-EM structure of the human snRNA export complex comprising CBC-PHAX-CRM1-RanGTP and…
5DIS 2.85 Å, Crystal structure of a CRM1-RanGTP-SPN1 export complex bound to a 113 amino acid…
3GB8 2.9 Å, Crystal structure of CRM1/Snurportin-1 complex
9B62 2.9 Å, Human RANBP2/RAN(GTP)/RANGAP1-SUMO1/UBC9/CRM1/RAN(GTP) - composite map and model
9OG9 2.93 Å, Cryo-EM structure of human full-length XPO1 (unliganded)
11RM 2.95 Å, Cryo-EM structure of human exportin-1 conjugated with FR-027*
6TVO 3.2 Å, Human CRM1-RanGTP in complex with Leptomycin B
9OGB 3.25 Å, Cryo-EM structure of human exportin-1 conjugated with selinexor and bound to yeast…
9OGE 3.28 Å, Cryo-EM structure of human exportin-1 conjugated with KPT-127 and bound to human…
9OGA 3.37 Å, Cryo-EM structure of human full-length XPO1 conjugated with selinexor

Browse structure collections

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