2X0Y: O-glcnacase nagj

Screening-based discovery of drug-like O-GlcNAcase inhibitor scaffolds. Determined by X-ray diffraction at 2.25 Å resolution. Released 12 Jan 2010.

Method: X-ray diffraction
Resolution: 2.25 Å
Organism: CLOSTRIDIUM PERFRINGENS
Chains: 2
Atoms: 10,123
Mol. weight: 133.89 kDa
Ligands: X0T
Released: 12 Jan 2010

Explore 2X0Y in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2X0Y contains 71 α-helices and 49 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: 35 helices, 25 β-strands

Element	Residues	Length	Sheet
α-helix	42-45	4
α-helix	49-50	2
β-strand	52-55	4	1
β-strand	60-61	2	2
α-helix	62-63	2
β-strand	65-66	2	3
β-strand	67-69	3	1
α-helix	76-88	13
β-strand	92-93	2	3
α-helix	94	1
β-strand	103-108	6	1
α-helix	114-120	7
β-strand	133-138	6	1
β-strand	141-146	6	1
α-helix	149-162	14
β-strand	164	1	2
β-strand	167-168	2	2
β-strand	171-175	5	1
β-strand	181-185	5	4
α-helix	192-194	3
α-helix	195-208	14
β-strand	212-215	4	4
α-helix	221-223	3
α-helix	230-232	3
α-helix	233-248	16
β-strand	252-257	6	4
α-helix	259-261	3
α-helix	267-285	19
β-strand	291-295	5	4
α-helix	304-314	11
α-helix	315-320	6
α-helix	321-322	2
α-helix	326-328	3
β-strand	329-331	3	4
α-helix	337-340	4
β-strand	341-342	2	5
β-strand	345-346	2	5
α-helix	348-356	9
β-strand	362-365	4	4
β-strand	375	1	6
α-helix	377-387	11
α-helix	390	1
β-strand	391-395	5	4
β-strand	415	1	6
α-helix	419-421	3
β-strand	423-428	6	4
α-helix	434-449	16
α-helix	456-468	13
α-helix	469-471	3
α-helix	472-479	8
β-strand	485-486	2	7
β-strand	492-493	2	7
α-helix	496	1
α-helix	499-513	15
α-helix	519-542	24
α-helix	545-576	32
α-helix	580-599	20
α-helix	606-610	5
α-helix	611-618	8
α-helix	621-623	3

Chain B: 36 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	41-45	5
α-helix	49-50	2
β-strand	52-55	4	8
β-strand	60-61	2	9
α-helix	62-63	2
β-strand	65-69	5	8
α-helix	76-88	13
β-strand	92-93	2	8
α-helix	94	1
β-strand	102-108	7	8
α-helix	114-120	7
α-helix	129	1
β-strand	133-138	6	8
β-strand	141-146	6	8
α-helix	149-162	14
β-strand	164	1	9
β-strand	167-168	2	9
β-strand	171-175	5	8
β-strand	181-185	5	10
α-helix	192-194	3
α-helix	195-208	14
β-strand	212-215	4	10
α-helix	221-223	3
α-helix	230-232	3
α-helix	233-248	16
β-strand	252-257	6	10
α-helix	259-261	3
α-helix	267-286	20
β-strand	291-295	5	10
α-helix	304-314	11
α-helix	315-320	6
α-helix	321-322	2
α-helix	325-328	4
β-strand	329-331	3	10
α-helix	337-340	4
β-strand	341-342	2	11
β-strand	345-346	2	11
α-helix	348-356	9
β-strand	362-365	4	10
β-strand	375	1	12
α-helix	377-387	11
β-strand	391-395	5	10
α-helix	410-412	3
β-strand	415	1	12
α-helix	419-421	3
β-strand	423-428	6	10
α-helix	437-449	13
α-helix	456-468	13
α-helix	469-471	3
α-helix	472-480	9
β-strand	485-486	2	13
β-strand	492-493	2	13
α-helix	495-496	2
α-helix	499-513	15
α-helix	519-542	24
α-helix	545-576	32
α-helix	580-599	20
α-helix	606-610	5
α-helix	611-618	8
α-helix	621-623	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
O-glcnacase nagj	A, B	protein	594	CLOSTRIDIUM PERFRINGENS	Q0TR53 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2X0Y_1 O-GLCNACASE NAGJ (chains A, B)
VGPKTGEENQVLVPNLNPTPENLEVVGDGFKITSSINLVGEEEADENAVNALREFLTANN
IEINSENDPNSTTLIIGEVDDDIPELDEALNGTTAENLKEEGYALVSNDGKIAIEGKDGD
GTFYGVQTFKQLVKESNIPEVNITDYPTVSARGIVEGFYGTPWTHQDRLDQIKFYGENKL
NTYIYAPKDDPYHREKWREPYPESEMQRMQELINASAENKVDFVFGISPGIDIRFDGDAG
EEDFNHLITKAESLYDMGVRSFAIYWDDIQDKSAAKHAQVLNRFNEEFVKAKGDVKPLIT
VPTEYDTGAMVSNGQPRAYTRIFAETVDPSIEVMWTGPGVVTNEIPLSDAQLISGIYNRN
MAVWWNYPVTDYFKGKLALGPMHGLDKGLNQYVDFFTVNPMEHAELSKISIHTAADYSWN
MDNYDYDKAWNRAIDMLYGDLAEDMKVFANHSTRMDNKTWAKSGREDAPELRAKMDELWN
KLSSKEDASALIEELYGEFARMEEACNNLKANLPEVALEECSRQLDELITLAQGDKASLD
MIVAQLNEDTEAYESAKEIAQNKLNTALSSFAVISEKVAQSFIQEALSFDLTLI

Ligands and cofactors

ID	Name	Formula	Copies
X0T	7-[(2S)-2,3-dihydroxypropyl]-1,3-dimethyl-3,7-dihydro-1H-purine-2,6-dione	C10 H14 N4 O4	2

Primary citation

Screening-Based Discovery of Drug-Like O-Glcnacase Inhibitor Scaffolds. Dorfmueller, H.C., Van Aalten, D.M.F. FEBS Lett (2010) 584:694. DOI 10.1016/J.FEBSLET.2009.12.020 · 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
2W1N 1.8 Å, cohesin and fibronectin type-III double module construct from the Clostridium…
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…
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…

Browse structure collections

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