6G0C: SdeA catalytic core

Crystal structure of SdeA catalytic core. Determined by X-ray diffraction at 2.8 Å resolution. Released 30 May 2018.

Method
X-ray diffraction
Resolution
2.8 Å
Organism
Legionella pneumophila
Chains
1
Atoms
4,863
Mol. weight
79.37 kDa
Ligands
1PS
Released
30 May 2018

Explore 6G0C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6G0C contains 36 α-helices and 23 β-strands across 1 chain. 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: 36 helices, 23 β-strands

ElementResiduesLengthSheet
α-helix227-2282
β-strand22911
α-helix238-25013
α-helix255-2562
α-helix263-2642
β-strand265-26732
β-strand270-27232
α-helix279-30224
α-helix315-3173
α-helix320-33112
α-helix344-36421
α-helix377-38812
α-helix391-3933
α-helix398-40811
α-helix409-4135
α-helix418-45134
α-helix455-4573
β-strand45913
β-strand46614
α-helix4671
β-strand468-46925
β-strand474-47525
β-strand47716
β-strand49815
β-strand51316
α-helix5141
β-strand51514
α-helix516-5216
α-helix523-5264
β-strand53613
α-helix545-5528
α-helix555-5628
α-helix564-58623
α-helix588-5936
α-helix596-5994
α-helix600-61415
α-helix616-6183
β-strand61917
β-strand624-62637
β-strand629-63137
α-helix633-64210
α-helix645-6506
α-helix654-66613
β-strand671-67228
α-helix679-6813
β-strand682-68328
α-helix684-6918
α-helix702-71312
α-helix716-72611
α-helix735-75622
β-strand763-76861
α-helix772-78716
β-strand821-82221
α-helix825-8262
α-helix827-8315
β-strand836-84161
β-strand86311
β-strand871-881111
β-strand890-899101

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitinating/deubiquitinating enzyme SdeAAprotein695Legionella pneumophilaQ5ZTK4 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6G0C_1 Ubiquitinating/deubiquitinating enzyme SdeA (chains A)
EMSVKPTAPQDKSVPVWNGFSLYTDDTVKAAAQYAYDNYLGKPYTGSVESAPANFGGRMV
YRQHHGLSHTLRTMAYAELIVEEARKAKLRGETLGKFKDGRTIADVTPQELKKIMIAQAF
FVAGRDDEASDAKNYQKYHEQSRDAFLKYVKDNESTLIPDVFKDQEDVNFYARVIEDKSH
DWESTPAHVLINQGHMVDLVRVKQPPESFLQRYFSSMQRWIGSQATEAVFGIQRQFFHAT
YEVVAGFDSDNKEPHLVVSGLGRYVIGEDGQPIREAPKKGQKEGDLKVFPQTYKLKENER
LMRVDEFLKLPEIQNTFPGSGKHLQGGMPGMNEMDYWNRLNSLNRARCENDVDFCLKQLQ
TAHDKAKIEPIKQAFQSSKGKERRQPNVDEIAAARIIQQILANPDCIHDDHVLINGQKLE
QQFFRDLLAKCEMAVVGSLLNDTDIGNIDTLMRHEKDTEFHSTNPEAVPVKIGEYWINDQ
RINNSSGNITQKKHDLIFLMQNDAWYFSRVNAIAQNRDKGSTFKEVLITTLMTPLTSKAL
VDTSQAKPPTRLFRGLNLSEEFTKGLIDQANAMIANTTERLFTDHSPEAFKQIKLNDLSK
MSGRTNASTTTEIKLVKETWDSNVIFEMLDPDGLLHSKQVGRHGEGTESEFSVYLPEDVA
LVPVKVTLDGKTQKGENRYVFTFVAVKSPDFTPRH

Ligands and cofactors

IDNameFormulaCopies
1PS3-pyridinium-1-ylpropane-1-sulfonateC8 H11 N O3 S1

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

Primary citation

Insights into catalysis and function of phosphoribosyl-linked serine ubiquitination. Kalayil, S., Bhogaraju, S., Bonn, F. et al. Nature (2018) 557:734-738. DOI 10.1038/s41586-018-0145-8 · PubMed

Other PDB entries of the same protein (UniProt Q5ZTK4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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