7B51: GTP-binding nuclear protein Ran

Crystal structure of human CRM1 covalently modified by 2-mercaptoethanol at Cys528. Determined by X-ray diffraction at 2.58 Å resolution. Released 10 Mar 2021.

Method
X-ray diffraction
Resolution
2.58 Å
Organism
Homo sapiens
Chains
2
Atoms
9,786
Mol. weight
143.37 kDa
Ligands
MG, GTP
Released
10 Mar 2021

Explore 7B51 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7B51 contains 79 α-helices and 12 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: 70 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix10-134
α-helix14-174
α-helix22-232
α-helix25-3713
α-helix40-5516
α-helix59-624
α-helix63-697
α-helix73-9018
α-helix91-933
α-helix96-11520
α-helix117-1226
α-helix124-14522
α-helix149-15911
α-helix161-17919
α-helix188-20013
α-helix202-21514
α-helix219-23214
α-helix238-2425
α-helix246-2494
α-helix250-2556
α-helix258-2603
α-helix261-27313
α-helix280-29718
α-helix304-3107
α-helix313-33826
α-helix341-3433
α-helix344-35714
α-helix363-38321
α-helix404-4096
α-helix413-42311
α-helix424-4263
β-strand430-43454
β-strand440-44454
α-helix449-46719
α-helix469-48416
α-helix491-50313
α-helix510-53021
α-helix534-54916
α-helix552-5576
α-helix559-57214
α-helix580-59516
α-helix596-5994
α-helix602-6032
α-helix610-6156
α-helix618-6214
α-helix627-64216
α-helix647-65711
α-helix659-67416
α-helix676-6805
α-helix682-70221
α-helix704-7063
α-helix707-73529
α-helix738-7414
α-helix743-76523
α-helix769-7757
α-helix7801
α-helix781-7855
α-helix786-7905
α-helix793-7953
α-helix799-81113
α-helix813-8164
α-helix819-83113
α-helix842-85817
α-helix861-8655
α-helix868-88114
α-helix887-90418
α-helix908-93023
α-helix933-9386
α-helix939-95517
α-helix970-98516
α-helix991-100313
α-helix1008-102114
Chain B: 9 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand9-1791
α-helix23-3210
α-helix41-433
β-strand45-5281
β-strand53-5422
β-strand59-6681
α-helix70-723
α-helix76-805
β-strand85-9171
α-helix95-995
α-helix101-1099
β-strand117-12261
α-helix133-1353
α-helix138-1414
β-strand145-14841
β-strand15013
β-strand15513
α-helix159-16911
β-strand176-17722

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
GTP-binding nuclear protein RanBprotein182Homo sapiensP62826 (AlphaFold model)
Exportin-1Aprotein1060Homo sapiensO14980 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>7B51_1 GTP-binding nuclear protein Ran (chains B)
MGMAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGP
IKFNVWDTAGLEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIV
LCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVA
MP
Sequence of entity 2 (A), FASTA
>7B51_2 Exportin-1 (chains A)
MASMTGGQQMGRGSMPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMA
QEVLTHLKEHPDAWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYV
VGLIIKTSSDPTCVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQN
NMVILKLLSEEVFDFSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATL
ETLLRFLNWIPLGYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTL
FTLTMMQLKQMLPLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRET
LMEALHYMLLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRR
QLYLPMLFKVRLLMVSRMAKPEEAAAVENDQGEVVREFMKDTDSINLYKNMRETLVYLTH
LDYVDTERIMTEKLHNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLG
LCEQKRGKDNKAIIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACD
TFIKIAQKCRRHFVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTD
QTVQEHLIEKYMLLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPF
VIQLGRIYLDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRS
NDPQMVAENFVPPLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAV
FECTLNMINKDFEEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTM
RNVADTGLQILFTLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASIL
AYMFNLVEEGKISTSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQ
DIPAFKEHLRDFLVQIKEFAGEDTSDLFLERSRSHHHHHH

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1
GTPGuanosine-5'-triphosphateC10 H16 N5 O14 P31

Water and common crystallization additives (BME) are not listed.

Primary citation

Crystal structure of human CRM1, covalently modified by 2-mercaptoethanol on Cys528, in complex with RanGTP. Shaikhqasem, A., Schmitt, K., Valerius, O. et al. Acta Crystallogr F Struct Biol Commun (2021) 77:70-78. DOI 10.1107/S2053230X2100203X · PubMed

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

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