4GMN: Rpl5 recognition by Syo1

Structural basis of Rpl5 recognition by Syo1. Determined by X-ray diffraction at 2.95 Å resolution. Released 31 Oct 2012.

Method
X-ray diffraction
Resolution
2.95 Å
Organism
Chaetomium thermophilum
Chains
2
Atoms
4,451
Mol. weight
80.78 kDa
Released
31 Oct 2012

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

Secondary structure: helices and β-sheets

4GMN contains 43 α-helices and 4 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: 39 helices, 3 β-strands

ElementResiduesLengthSheet
α-helix37-437
α-helix48-6114
α-helix67-737
α-helix76-827
α-helix84-863
α-helix90-10617
α-helix110-1178
α-helix120-13617
α-helix142-1443
α-helix147-16822
α-helix172-1787
α-helix182-19413
α-helix199-21315
α-helix217-2248
α-helix231-24010
α-helix246-25914
β-strand26812
β-strand27212
α-helix274-2774
α-helix278-2836
α-helix3011
α-helix302-3065
α-helix307-32822
α-helix412-4165
α-helix417-4215
α-helix422-4309
α-helix436-45621
β-strand45911
α-helix467-47913
α-helix480-4856
α-helix486-4905
α-helix496-51318
α-helix523-53311
α-helix551-5533
α-helix555-56511
α-helix573-58816
α-helix590-5923
α-helix595-60814
α-helix615-6162
α-helix617-6226
α-helix626-64116
α-helix650-67122
Chain B: 4 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix51
β-strand611
α-helix71
α-helix10-167
α-helix18-192

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
60S ribosomal protein l5-like proteinBprotein49Chaetomium thermophilumG0SEG2 (AlphaFold model)
Putative uncharacterized proteinAprotein676Chaetomium thermophilumG0S5S6 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>4GMN_1 60S ribosomal protein l5-like protein (chains B)
MAFHKLVKNSAYYSRFQTKFKRRRQGKTDYYARKRLITQAKGSHHHHHH
Sequence of entity 2 (A), FASTA
>4GMN_2 Putative uncharacterized protein (chains A)
MGKTRRNRVRNRTDPIAKPVKPPTDPELAKLREDKILPVLKDLKSPDAKSRTTAAGAIAN
IVQDAKCRKLLLREQVVHIVLTETLTDNNIDSRAAGWEILKVLAQEEEADFCVHLYRLDV
LTAIEHAAKAVLETLTTSEPPFSKLLKAQQRLVWDITGSLLVLIGLLALARDEIHEAVAT
KQTILRLLFRLISADIAPQDIYEEAISCLTTLSEDNLKVGQAITDDQETHVYDVLLKLAT
GTDPRAVMACGVLHNVFTSLQWMDHSPGKDGACDAILIPTLTRALEHVVPGGAKFNGDAR
YANITLLALVTLASIGTDFQETLVKGNQGSRESPISAADEEWNGFDDADGDAMDVDQKSS
SGEDQEEDYEEIDVKEDDEDDDDDSITSEMQADMERVVGADGTDDGDLEDLPTLRELIQT
AVPQLIRLSNLPIDSDESLTIQSHALSALNNISWTISCLEFANGENANIHNAWYPTAKKI
WRKTILPILEADSADLKLATQVTSLAWAVARVLHGETPTDGNPHRKFISLYHSSKQQAGG
NSNSIEEPEDPFQGLGVKCIGVVGSLAHDPAPIEVNREVGVFLVTLLRQSNNVPPAEIVE
ALNQLFDIYGDEELACDKEVFWKDGFLKHLEEFLPKMRTLTKGIDKRTQPELRTRADEAL
LNLGRFVQYKKKHAPK

Primary citation

Synchronizing nuclear import of ribosomal proteins with ribosome assembly. Kressler, D., Bange, G., Ogawa, Y. et al. Science (2012) 338:666-671. DOI 10.1126/science.1226960 · PubMed

Other PDB entries of the same protein (UniProt G0SEG2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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