5WGB: Human mitochondrial Cysteine Desulfurase

Crystal Structure of the Human mitochondrial Cysteine Desulfurase in complex with ISD11 and E. coli ACP1 protein at 2.75A. Determined by X-ray diffraction at 2.75 Å resolution. Released 26 Jul 2017.

Method
X-ray diffraction
Resolution
2.75 Å
Organisms
Homo sapiens, Escherichia coli O45:K1 (strain S88 / ExPEC)
Chains
3
Atoms
3,247
Mol. weight
67.46 kDa
Ligands
8Q1, PLP
Released
26 Jul 2017

Explore 5WGB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5WGB contains 18 α-helices and 18 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: 12 helices, 16 β-strands

ElementResiduesLengthSheet
α-helix68-703
α-helix71-8111
α-helix98-11417
α-helix118-1203
β-strand121-12441
α-helix127-14115
β-strand148-15251
α-helix157-16812
β-strand172-17651
α-helix1771
β-strand17812
β-strand18412
α-helix186-1927
β-strand197-20151
β-strand20513
β-strand21114
β-strand21213
α-helix215-22511
β-strand228-23251
β-strand251-25551
β-strand266-27051
α-helix298-33639
β-strand341-34225
α-helix346-3483
β-strand34914
β-strand353-35755
β-strand405-40955
α-helix416-42712
Chain B: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix7-2014
α-helix26-4217
α-helix49-7527
Chain C: 3 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix8-158
β-strand2716
α-helix36-5015
β-strand6416
α-helix65-728

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cysteine desulfurase, mitochondrialAprotein426Homo sapiensQ9Y697 (AlphaFold model)
LYR motif-containing protein 4Bprotein91Homo sapiensQ9HD34 (AlphaFold model)
Acyl carrier proteinCprotein77Escherichia coli O45:K1 (strain S88 / ExPEC)B7MJ81 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5WGB_1 Cysteine desulfurase, mitochondrial (chains A)
MGSSHHHHHHSSGLVPRGSHMLEMLRPLYMDVQATTPLDPRVLDAMLPYLINYYGNPHSR
THAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGVARFYRSRKKHLIT
TQTEHKCVLDSCRSLEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGV
KQPIAEIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIR
RRPRVRVEALQSGGGQERGMRSGTVPTPLVVGLGAACEVAQQEMEYDHKRISKLSERLIQ
NIMKSLPDVVMNGDPKHHYPGCINLSFAYVEGESLLMALKDVALSSGSACTSASLEPSYV
LRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTVEKCIQHVKRLREMSPLWEMVQDGIDLKS
IKWTQH
Sequence of entity 2 (B), FASTA
>5WGB_2 LYR motif-containing protein 4 (chains B)
MAASSRAQVLALYRAMLRESKRFSAYNYRTYAVRRIRDAFRENKNVKDPVEIQTLVNKAK
RDLGVIRRQVHIGQLYSTDKLIIENRDMPRT
Sequence of entity 3 (C), FASTA
>5WGB_3 Acyl carrier protein (chains C)
STIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEAE
KITTVQAAIDYINGHQA

Ligands and cofactors

IDNameFormulaCopies
8Q1S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}ami…C23 H45 N2 O8 P S1
PLPPyridoxal-5'-phosphateC8 H10 N O6 P1

Primary citation

Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex. Boniecki, M.T., Freibert, S.A., Muhlenhoff, U. et al. Nat Commun (2017) 8:1287-1287. DOI 10.1038/s41467-017-01497-1 · PubMed

Other PDB entries of the same protein (UniProt Q9Y697 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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