11LJ: Human oga

Human oga in complex with ligand 24. Determined by X-ray diffraction at 2.33 Å resolution. Released 1 Jul 2026.

Method: X-ray diffraction
Resolution: 2.33 Å
Organism: Homo sapiens
Chains: 4
Atoms: 7,063
Mol. weight: 126.91 kDa
Ligands: CA, A1DE3
Released: 1 Jul 2026

Explore 11LJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

11LJ contains 46 α-helices and 20 β-strands across 4 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: 16 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	61-66	6	1
α-helix	72-73	2
α-helix	75-87	13
β-strand	92-95	4	1
α-helix	101-103	3
α-helix	110-111	2
α-helix	113-128	16
β-strand	132-137	6	1
α-helix	148-163	16
β-strand	168-172	5	1
α-helix	182-185	4
α-helix	191-205	15
β-strand	212-215	4	1
α-helix	232-240	9
β-strand	245-249	5	1
α-helix	261-271	11
α-helix	274-275	2
β-strand	276-279	4	1
α-helix	301-306	6
β-strand	309-312	4	1
α-helix	319-321	3
α-helix	322-334	13
α-helix	376-388	13
α-helix	389-392	4

Chain B: 15 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	61-66	6	3
α-helix	72-73	2
α-helix	75-87	13
β-strand	92-95	4	3
α-helix	101-103	3
α-helix	110-112	3
α-helix	113-128	16
β-strand	132-137	6	3
α-helix	148-162	15
β-strand	168-172	5	3
α-helix	191-205	15
β-strand	212-215	4	3
α-helix	232-240	9
β-strand	246-249	4	3
α-helix	261-271	11
α-helix	274-275	2
β-strand	276-279	4	3
α-helix	301-306	6
β-strand	309-312	4	3
α-helix	319-321	3
α-helix	322-333	12
α-helix	376-387	12
α-helix	388-390	3

Chain C: 7 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	546-548	3
α-helix	551-553	3
α-helix	555-564	10
β-strand	567	1	2
β-strand	570	1	2
α-helix	573-581	9
α-helix	606-628	23
α-helix	634-661	28
α-helix	685-690	6

Chain D: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	545-548	4
α-helix	550-554	5
α-helix	555-564	10
β-strand	567	1	4
β-strand	570	1	4
α-helix	573-587	15
α-helix	589-592	4
α-helix	604-629	26
α-helix	634-661	28
α-helix	684-689	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein O-GlcNAcase N-Terminal Fragment	A, B	protein	386	Homo sapiens	O60502 (AlphaFold model)
Protein O-GlcNAcase 535-704 Peptide	C, D	protein	170	Homo sapiens	O60502 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>11LJ_1 Protein O-GlcNAcase N-Terminal Fragment (chains A, B)
EERESELSSNPAASAGASLEPPAAPAPGEDNPAGAGGAAVAGAAGGARRFLCGVVEGFYG
RPWVMEQRKELFRRLQKWELNTYLYAPKDDYKHRMFWREMYSVEEAEQLMTLISAAREYE
IEFIYAISPGLDITFSNPKEVSTLKRKLDQVSQFGCRSFALLFDDIDHNMCAADKEVFSS
FAHAQVSITNEIYQYLGEPETFLFCPTEYCGTFCYPNVSQSPYLRTVGEKLLPGIEVLWT
GPKVVSKEIPVESIEEVSKIIKRAPVIWDNIHANDYDQKRLFLGPYKGRSTELIPRLKGV
LTNPNCEFEANYVAIHTLATWYKSNMNGVRKDVVMTDSEDSTVSIQIKLENEGSDEDIET
DVLYSPQMALKLALTEWLQEFGVPHQ

Sequence of entity 2 (C, D), FASTA

>11LJ_2 Protein O-GlcNAcase 535-704 Peptide (chains C, D)
KEQFVPGPNEKPLYTAEPVTLEDLQLLADLFYLPYEHGPKGAQMLREFQWLRANSSVVSV
NCKGKDSEKIEEWRSRAAKFEEMCGLVMGMFTRLSNCANRTILYDMYSYVWDIKSIMSMV
KSFVQWLGCRSHSSAQFLIGDQEPWAFRGGLAGEFQRLLPIDGANDLFFQ

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2
A1DE3	N,N-dimethyl-2-(4-{[4-methyl-2-(propan-2-yl)pyridin-3-yl]amino}-1H-pyrrolo[3,2-…	C20 H25 N5 O	2

Primary citation

Discovery of 5‐Azaindole Inhibitors of O‐GlcNAcase for the Treatment of Alzheimer's Disease and Related Tauopathies. Bouton, J., Bretteville, A., Tresadern, G. et al. ACS Med Chem Lett (2026) 17:1096-1105. DOI 10.1021/acsmedchemlett.6c00017 · PubMed

Other PDB entries of the same protein (UniProt O60502 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5UN8 2.13 Å, Crystal Structure of human O-GlcNAcase in complex with glycopeptide p53
5M7U 2.3 Å, Structure of human O-GlcNAc hydrolase with new iminocyclitol type inhibitor
5M7R 2.35 Å, Structure of human O-GlcNAc hydrolase
5M7S 2.4 Å, Structure of human O-GlcNAc hydrolase with bound transition state analog ThiametG
7OU6 2.41 Å, Human O-GlcNAc hydrolase in complex with DNJNAc-thiazolidines
5TKE 2.48 Å, Crystal Structure of Eukaryotic Hydrolase
5UN9 2.5 Å, The crystal structure of human O-GlcNAcase in complex with Thiamet-G
8P0L 2.5 Å, Crystal structure of human O-GlcNAcase in complex with an S-linked CKII peptide
9BA8 2.54 Å, O-GlcNAcase (OGA) inhibitor complex for the Treatment of Alzheimer's Disease
2YDQ 2.6 Å, CpOGA D298N in complex with hOGA-derived O-GlcNAc peptide
5M7T 2.6 Å, Structure of human O-GlcNAc hydrolase with PugNAc type inhibitor
5VVO 2.6 Å, Structural Investigations of the Substrate Specificity of Human O-GlcNAcase

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