2OZN: O-GlcNAcase nagJ

The Cohesin-Dockerin Complex of NagJ and NagH from Clostridium perfringens. Determined by X-ray diffraction at 1.6 Å resolution. Released 6 May 2008.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
Clostridium perfringens
Chains
2
Atoms
2,313
Mol. weight
33.11 kDa
Ligands
CA
Released
6 May 2008

Explore 2OZN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2OZN contains 6 α-helices and 15 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: 1 helix, 12 β-strands

ElementResiduesLengthSheet
β-strand776-78271
β-strand786-78832
β-strand792-803121
β-strand809-81572
β-strand821-82771
β-strand832-84092
β-strand843-85082
α-helix855-8573
β-strand861-86991
β-strand873-886142
β-strand892-89432
β-strand89611
β-strand898-90582
Chain B: 5 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix1500-151516
β-strand151813
β-strand152513
α-helix1529-154416
α-helix1551-157020
β-strand157213
α-helix1588-15969
α-helix1616-162712

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
O-GlcNAcase nagJAprotein165Clostridium perfringensQ0TR53 (AlphaFold model)
HyalurononglucosaminidaseBprotein140Clostridium perfringensP26831 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2OZN_1 O-GlcNAcase nagJ (chains A)
MGSSHHHHHHSSGLVPRGSHMASKLKENAEVTGSVSLEALEEVQVGENLEVGVGIDELVN
AEAFAYDFTLNYDENAFEYVEAISDDGVFVNAKKIEDGKVRVLVSSLTGEPLPAKEVLAK
VVLRAEAKAEGSNLSVTNSSVGDGEGLVHEIAGTEKTVNIIEGTS
Sequence of entity 2 (B), FASTA
>2OZN_2 Hyalurononglucosaminidase (chains B)
MDKTNLGELINQGKSLLDESVEGFNVGEYHKGAKDGLTVEINKAEEVFNKEDATEEEINL
AKESLEGAIARFNSLLIEESTGDFNGNGKIDIGDLAMVSKNIGSTTNTSLDLNKDGSIDE
YEISFINHRILNLEHHHHHH

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa2

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

Primary citation

Structural basis of Clostridium perfringens toxin complex formation. Adams, J.J., Gregg, K., Bayer, E.A. et al. Proc Natl Acad Sci U S A (2008) 105:12194-12199. DOI 10.1073/pnas.0803154105 · PubMed

Other PDB entries of the same protein (UniProt Q0TR53 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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