2W1N: O-glcnacase nagj

Name: PDB 2W1N: cohesin and fibronectin type-III double module construct from the Clostridium perfringens glycoside hydrolase GH84C
Published: 2009-02-03
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: hydrolase

cohesin and fibronectin type-III double module construct from the Clostridium perfringens glycoside hydrolase GH84C. Determined by X-ray diffraction at 1.8 Å resolution. Released 3 Feb 2009.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: CLOSTRIDIUM PERFRINGENS
Chains: 1
Atoms: 2,070
Mol. weight: 25.98 kDa
Released: 3 Feb 2009

Explore 2W1N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2W1N contains 4 α-helices and 20 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: 4 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	776-782	7	1
β-strand	786-788	3	2
β-strand	792-803	12	1
β-strand	809-815	7	2
β-strand	821-827	7	1
β-strand	832-840	9	2
β-strand	843-850	8	2
α-helix	855-857	3
β-strand	861-869	9	1
β-strand	873-886	14	2
β-strand	892-894	3	2
β-strand	896	1	1
β-strand	898-905	8	2
α-helix	908-911	4
β-strand	918-925	8	3
β-strand	930-935	6	3
β-strand	943-950	8	4
β-strand	953-959	7	4
β-strand	964-967	4	3
α-helix	970-971	2
β-strand	975-984	10	4
β-strand	989	1	4
α-helix	990-992	3
β-strand	993-998	6	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
O-glcnacase nagj	A	protein	238	CLOSTRIDIUM PERFRINGENS	Q0TR53 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2W1N_1 O-GLCNACASE NAGJ (chains A)
MVHGKLKEAAEVTGSVSLEALEEVQVGENIEVGVGIDELVNAEAFAYDFTLNYDENAFEY
VEAISDDGVFVNAKKIEDGKVRVLVSSLTGEPLPAKEVLAKVVLRAEAKTEGSNLSVTNS
SVGDGEGLVHEIAGTEKTVNIIEGTSPEIVVNPVRDFKASEINKKNVTVTWTEPETTEGL
EGYILYKDGKKVAEIGKDETSYTFKKLNRHTIYNFKIAAKYSNGEVSSKESLTLRTAR

Primary citation

Portrait of an Enzyme: A Complete Structural Analysis of a Multi-Modular Beta-N-Acetylglucosaminidase from Clostridium Perfringens. Ficko-Blean, E., Gregg, K.J., Adams, J.J. et al. J Biol Chem (2009) 284:9876. DOI 10.1074/JBC.M808954200 · PubMed

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

2J1A 1.49 Å, Structure of CBM32 from Clostridium perfringens beta-N- acetylhexosaminidase GH84C in…
2OZN 1.6 Å, The Cohesin-Dockerin Complex of NagJ and NagH from Clostridium perfringens
2V5C 2.1 Å, Family 84 glycoside hydrolase from Clostridium perfringens, 2.1 Angstrom structure
2VUR 2.2 Å, Chemical dissection of the link between Streptozotocin, O-GlcNAc and pancreatic cell death
2CBI 2.25 Å, Structure of the Clostridium perfringens NagJ family 84 glycoside hydrolase, a homologue…
2X0Y 2.25 Å, Screening-based discovery of drug-like O-GlcNAcase inhibitor scaffolds
2J62 2.26 Å, Structure of a bacterial O-glcnacase in complex with glcnacstatin
2J7M 2.3 Å, Characterization of a Family 32 CBM
7KHV 2.3 Å, Cpoga in complex with ligand 54
2WB5 2.31 Å, GlcNAcstatins are nanomolar inhibitors of human O-GlcNAcase inducing cellular…
2CBJ 2.35 Å, Structure of the Clostridium perfringens NagJ family 84 glycoside hydrolase, a homologue…
2J1E 2.4 Å, High Resolution Crystal Structure of CBM32 from a N-acetyl-beta- hexosaminidase in…

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