Current Protein Identity:O60502 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
2YDQ CpOGA D298N in complex with hOGA-derived O-GlcNAc peptide Deposited 2011-03-24 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain T 402–408(7 aa) Fragment:HOGA O-GLCNAC PEPTIDE, RESIDUES 402-408
Not recorded CD CADMIUM ION × 19 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5;0.6M NAAC, 0.175M CDSO4, 0.1M HEPES PH 7.5
Resolution 2.60 Å R-free 0.231
5M7R Structure of human O-GlcNAc hydrolase Deposited 2016-10-28 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–916(916 aa)
Chain B 1–916(916 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;292 K;0.14 - 0.2 M triammonium citrate pH 7.5, 16-20 % PEG 3350
Resolution 2.35 Å R-free 0.249
5M7S Structure of human O-GlcNAc hydrolase with bound transition state analog ThiametG Deposited 2016-10-28 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–916(916 aa)
Chain B 1–916(916 aa)
Not recorded NHT (3AR,5R,6S,7R,7AR)-2-(ETHYLAMINO)-5-(HYDROXYMETHYL)-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D][1,3]THIAZOLE-6,7-DIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;292 K;0.1-0.2 M tri ammonium citrate pH 7.5 16-20 % PEG 3350
Resolution 2.40 Å R-free 0.232
5M7T Structure of human O-GlcNAc hydrolase with PugNAc type inhibitor Deposited 2016-10-28 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–916(916 aa)
Chain B 1–916(916 aa)
Not recorded GDV (5R,6R,7R,8S)-8-(ACETYLAMINO)-6,7-DIHYDROXY-5-(HYDROXYMETHYL)-N-PHENYL-1,5,6,7,8,8A-HEXAHYDROIMIDAZO[1,2-A]PYRIDINE-2-CARBOXAMIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;292 K;0.1-0.2 M tri Ammonium citrate 16-20 % PEG 3350
Resolution 2.60 Å R-free 0.235
5M7U Structure of human O-GlcNAc hydrolase with new iminocyclitol type inhibitor Deposited 2016-10-28 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–916(916 aa)
Chain B 1–916(916 aa)
Not recorded XHA 2-[(2~{R},3~{S},4~{R},5~{R})-5-(hydroxymethyl)-3,4-bis(oxidanyl)-1-[3-[3-(trifluoromethyl)phenyl]propyl]pyrrolidin-2-yl]-~{N}-methyl-ethanamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;292 K;0.1-0.2 M tri Ammonium citrate pH 7.5 16-20 % PEG 3350
Resolution 2.30 Å R-free 0.227
5TKE Crystal Structure of Eukaryotic Hydrolase Deposited 2016-10-06 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 60–400(341 aa) Fragment:unp residues 60-542; unp residues 553-704
Chain A 553–704(152 aa) Fragment:unp residues 60-542; unp residues 553-704
Chain B 60–400(341 aa) Fragment:unp residues 60-542; unp residues 553-704
Chain B 553–704(152 aa) Fragment:unp residues 60-542; unp residues 553-704
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION;pH 7;293 K;0.032 M ammonium citrate tribasic (pH 7.0), 0.02 M MES monohydrate, 0.016 M imidazole, 0.002 M zinc sulfate heptahydrate, 0.128 M potassium thiocyanate, 12.8% w/v polyethylene glycol 3,350, 3.2% w/v polyethylene glycol monomethyl ether 2,000, and 5% w/v polyethylene glycol monomethyl ether 550
Resolution 2.48 Å R-free 0.236
5UHK Crystal structure of the core catalytic domain of Human O-GlcNAcase Deposited 2017-01-11 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 56–400(345 aa)
Chain B 544–705(162 aa)
Chain C 56–400(345 aa)
Chain D 544–705(162 aa)
Not recorded GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;293 K;14-17% PEG 3350, 0.2 M Mg Formate
Resolution 2.97 Å R-free 0.251
5UHL Crystal structure of the core catalytic domain of human O-GlcNAcase complexed with Thiamet G Deposited 2017-01-11 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 56–400(345 aa)
Chain B 544–705(162 aa)
Chain C 56–400(345 aa)
Chain D 544–705(162 aa)
Not recorded 8BJ (2Z,3aR,5R,6S,7R,7aR)-2-(ethylimino)-5-(hydroxymethyl)hexahydro-3aH-pyrano[3,2-d][1,3]thiazole-6,7-diol × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;293 K;14-17% PEG 3350, 0.2 M Mg Formate
Resolution 3.14 Å R-free 0.257
5UHO Crystal structure of the core catalytic domain of human O-GlcNAcase complexed with PUGNAc Deposited 2017-01-11 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 56–400(345 aa)
Chain B 544–705(162 aa)
Chain C 56–400(345 aa)
Chain D 544–705(162 aa)
Not recorded OAN O-(2-ACETAMIDO-2-DEOXY D-GLUCOPYRANOSYLIDENE) AMINO-N-PHENYLCARBAMATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;293 K;14-17% PEG 3350, 0.2 M Mg Formate
Resolution 3.21 Å R-free 0.259
5UHP Crystal structure of the core catalytic domain of human O-GlcNAcase Deposited 2017-01-11 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 14–400(387 aa)
Chain B 14–400(387 aa)
Chain F 554–705(152 aa)
Chain G 554–705(152 aa)
Not recorded GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M K Na tartrate tetrahydrate, 20% PEG 3350
Resolution 2.79 Å R-free 0.292
5UHP Crystal structure of the core catalytic domain of human O-GlcNAcase Deposited 2017-01-11 Assembly 2 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain C 14–400(387 aa)
Chain D 14–400(387 aa)
Chain E 554–705(152 aa)
Chain H 554–705(152 aa)
Not recorded GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M K Na tartrate tetrahydrate, 20% PEG 3350
Resolution 2.79 Å R-free 0.292
5UN8 Crystal Structure of human O-GlcNAcase in complex with glycopeptide p53 Deposited 2017-01-30 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 60–400(341 aa) Fragment:UNP residues 60-400 and 553-704
Chain A 553–704(152 aa) Fragment:UNP residues 60-400 and 553-704
Chain C 60–400(341 aa) Fragment:UNP residues 60-400 and 553-704
Chain C 553–704(152 aa) Fragment:UNP residues 60-400 and 553-704
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION;293 K;0.032 M ammonium citrate tribasic (pH 7.0), 0.02 M MES monohydrate, 0.016 M imidazole, 0.002 M zinc sulfate heptahydrate, 0.128 M potassium thiocyanate, 12.8% w/v polyethylene glycol 3,350, 3.2% w/v polyethylene glycol monomethyl ether 2,000, and 5% w/v polyethylene glycol monomethyl ether 550.
Resolution 2.13 Å R-free 0.229
5UN8 Crystal Structure of human O-GlcNAcase in complex with glycopeptide p53 Deposited 2017-01-30 Assembly 2 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain B 60–400(341 aa) Fragment:UNP residues 60-400 and 553-704
Chain B 553–704(152 aa) Fragment:UNP residues 60-400 and 553-704
Chain D 60–400(341 aa) Fragment:UNP residues 60-400 and 553-704
Chain D 553–704(152 aa) Fragment:UNP residues 60-400 and 553-704
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION;293 K;0.032 M ammonium citrate tribasic (pH 7.0), 0.02 M MES monohydrate, 0.016 M imidazole, 0.002 M zinc sulfate heptahydrate, 0.128 M potassium thiocyanate, 12.8% w/v polyethylene glycol 3,350, 3.2% w/v polyethylene glycol monomethyl ether 2,000, and 5% w/v polyethylene glycol monomethyl ether 550.
Resolution 2.13 Å R-free 0.229
5UN9 The crystal structure of human O-GlcNAcase in complex with Thiamet-G Deposited 2017-01-30 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 60–400(341 aa) Fragment:UNP residues 60-400 and 553-704
Chain A 553–704(152 aa) Fragment:UNP residues 60-400 and 553-704
Chain B 60–400(341 aa) Fragment:UNP residues 60-400 and 553-704
Chain B 553–704(152 aa) Fragment:UNP residues 60-400 and 553-704
Not recorded NHT (3AR,5R,6S,7R,7AR)-2-(ETHYLAMINO)-5-(HYDROXYMETHYL)-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D][1,3]THIAZOLE-6,7-DIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION;293 K;0.128 M potassium thiocyanate, 0.032 M ammonium citrate tribasic (pH 7.0), 0.016 M imidazole (pH 7.0), 0.002 M zinc sulfate heptahydrate, 0.02 M MES monohydrate (pH 6.5), 12.8% w/v polyethylene glycol 3,350, 3.2% w/v polyethylene glycol monomethyl ether 2,000, 5% v/v polyethylene glycol monomethyl ether 550
Resolution 2.50 Å R-free 0.260
5VVO Structural Investigations of the Substrate Specificity of Human O-GlcNAcase Deposited 2017-05-19 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 60–400(341 aa) Fragment:UNP residues 60-400, 553-704
Chain A 553–704(152 aa) Fragment:UNP residues 60-400, 553-704
Chain B 60–400(341 aa) Fragment:UNP residues 60-400, 553-704
Chain B 553–704(152 aa) Fragment:UNP residues 60-400, 553-704
Mutation:D175N Mutation:D175N Mutation:D175N Mutation:D175N No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION;293 K;0.024 M ammonium citrate tribasic (pH 7.0), 0.015 M MES monohydrate, 0.096 M potassium thiocyanate, 0.25 M Sodium acetate trihydrate, 0.037 M imidazole, 0.002 M zinc sulfate heptahydrate, 9.6 % w/v polyethylene glycol 3,350, 2.4 % w/v polyethylene glycol monomethyl ether 2,000, and 4% w/v polyethylene glycol monomethyl ether 550
Resolution 2.60 Å R-free 0.259
5VVT Structural Investigations of the Substrate Specificity of Human O-GlcNAcase Deposited 2017-05-20 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 60–400(341 aa)
Chain A 553–704(152 aa)
Chain C 60–400(341 aa)
Chain C 553–704(152 aa)
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION;293 K;0.024 M ammonium citrate tribasic (pH 7.0), 0.015 M MES monohydrate, 0.096 M potassium thiocyanate, 0.25 M Sodium acetate trihydrate, 0.037 M imidazole, 0.002 M zinc sulfate heptahydrate, 9.6 % w/v polyethylene glycol 3,350, 2.4 % w/v polyethylene glycol monomethyl ether 2,000, and 4% w/v polyethylene glycol monomethyl ether 550
Resolution 2.80 Å R-free 0.291
5VVU Structural Investigations of the Substrate Specificity of Human O-GlcNAcase Deposited 2017-05-20 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 60–400(341 aa) Fragment:UNP residues 60-400, 553-704
Chain A 553–704(152 aa) Fragment:UNP residues 60-400, 553-704
Chain C 60–400(341 aa) Fragment:UNP residues 60-400, 553-704
Chain C 553–704(152 aa) Fragment:UNP residues 60-400, 553-704
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION;293 K;0.024 M ammonium citrate tribasic (pH 7.0), 0.015 M MES monohydrate, 0.096 M potassium thiocyanate, 0.25 M Sodium acetate trihydrate, 0.037 M imidazole, 0.002 M zinc sulfate heptahydrate, 9.6 % w/v polyethylene glycol 3,350, 2.4 % w/v polyethylene glycol monomethyl ether 2,000, and 4% w/v polyethylene glycol monomethyl ether 550
Resolution 2.70 Å R-free 0.275
5VVV Structural Investigations of the Substrate Specificity of Human O-GlcNAcase Deposited 2017-05-20 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 60–400(341 aa) Fragment:UNP residues 60-400, 553-704
Chain A 553–704(152 aa) Fragment:UNP residues 60-400, 553-704
Chain C 60–400(341 aa) Fragment:UNP residues 60-400, 553-704
Chain C 553–704(152 aa) Fragment:UNP residues 60-400, 553-704
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION;293 K;0.024 M ammonium citrate tribasic (pH 7.0), 0.015 M MES monohydrate, 0.096 M potassium thiocyanate, 0.25 M Sodium acetate trihydrate, 0.037 M imidazole, 0.002 M zinc sulfate heptahydrate, 9.6 % w/v polyethylene glycol 3,350, 2.4 % w/v polyethylene glycol monomethyl ether 2,000, and 4% w/v polyethylene glycol monomethyl ether 550
Resolution 2.80 Å R-free 0.257
5VVX Structural Investigations of the Substrate Specificity of Human O-GlcNAcase Deposited 2017-05-21 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 60–400(341 aa) Fragment:UNP residues 60-400, 553-704
Chain A 553–704(152 aa) Fragment:UNP residues 60-400, 553-704
Chain C 60–400(341 aa) Fragment:UNP residues 60-400, 553-704
Chain C 553–704(152 aa) Fragment:UNP residues 60-400, 553-704
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION;293 K;0.024 M ammonium citrate tribasic (pH 7.0), 0.015 M MES monohydrate, 0.096 M potassium thiocyanate, 0.25 M Sodium acetate trihydrate, 0.037 M imidazole, 0.002 M zinc sulfate heptahydrate, 9.6 % w/v polyethylene glycol 3,350, 2.4 % w/v polyethylene glycol monomethyl ether 2,000, and 4% w/v polyethylene glycol monomethyl ether 550
Resolution 2.90 Å R-free 0.282
6HKI Crystal structure of surface entropy mutant of human O-GlcNAc hydrolase Deposited 2018-09-06 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–916(916 aa)
Chain B 1–916(916 aa)
Mutation:E602A, E605A Mutation:E602A, E605A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;291 K;0.2 M sodium citrate tribasic, 17% polyethylene glycol 3350
Resolution 3.30 Å R-free 0.234
6PM9 Crystal structure of the core catalytic domain of human O-GlcNAcase bound to MK-8719 Deposited 2019-07-01 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 14–400(387 aa)
Chain B 14–400(387 aa)
Chain F 554–705(152 aa)
Chain G 554–705(152 aa)
Not recorded OQ1 (3aR,5S,6S,7R,7aR)-5-(difluoromethyl)-2-(ethylamino)-5,6,7,7a-tetrahydro-3aH-pyrano[3,2-d][1,3]thiazole-6,7-diol × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M K-Na-tartrate tetrahydrate, 20% (w/v) PEG 3350
Resolution 2.86 Å R-free 0.309
6PM9 Crystal structure of the core catalytic domain of human O-GlcNAcase bound to MK-8719 Deposited 2019-07-01 Assembly 2 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain C 14–400(387 aa)
Chain D 14–400(387 aa)
Chain E 554–705(152 aa)
Chain H 554–705(152 aa)
Not recorded OQ1 (3aR,5S,6S,7R,7aR)-5-(difluoromethyl)-2-(ethylamino)-5,6,7,7a-tetrahydro-3aH-pyrano[3,2-d][1,3]thiazole-6,7-diol × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M K-Na-tartrate tetrahydrate, 20% (w/v) PEG 3350
Resolution 2.86 Å R-free 0.309
7OU6 Human O-GlcNAc hydrolase in complex with DNJNAc-thiazolidines Deposited 2021-06-11 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain AAA 1–916(916 aa)
Chain BBB 1–916(916 aa)
Not recorded 1XI ~{N}-[(3~{Z},6~{S},7~{R},8~{R},8~{a}~{S})-7,8-bis(oxidanyl)-3-(phenylmethyl)imino-1,5,6,7,8,8~{a}-hexahydro-[1,3]thiazolo[3,4-a]pyridin-6-yl]ethanamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;291.15 K;0.14 - 0.2 M triammonium citrate pH 7.5, 16-20 % PEG 3350
Resolution 2.41 Å R-free 0.271
7YEH Cryo-EM structure of human OGT-OGA complex Deposited 2022-07-05 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain C 1–916(916 aa)
Chain D 1–916(916 aa)
Not recorded UDP URIDINE-5'-DIPHOSPHATE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.92 Å
8P0L Crystal structure of human O-GlcNAcase in complex with an S-linked CKII peptide Deposited 2023-05-10 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–916(916 aa)
Chain B 1–916(916 aa)
Not recorded CYS CYSTEINE × 1 SER SERINE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;291.15 K;0.14 - 0.2 M triammonium citrate pH 7.5, 16-20 % PEG 3350
Resolution 2.50 Å R-free 0.271
9BA8 O-GlcNAcase (OGA) inhibitor complex for the Treatment of Alzheimer's Disease Deposited 2024-04-03 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 55–713(659 aa)
Chain B 55–713(659 aa)
Not recorded A1AKM N-[4-fluoro-5-({(2S,4S)-2-methyl-4-[(5-methyl-1,2,4-oxadiazol-3-yl)methoxy]piperidin-1-yl}methyl)-1,3-thiazol-2-yl]acetamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7;294 K;15% PEG 3350, 200mM Magnesium Chloride, 100mM Hepes pH 7.0, 5% DMSO
Resolution 2.54 Å R-free 0.231
9BA9 O-GlcNAcase (OGA) inhibitor complex for the Treatment of Alzheimer's Disease Deposited 2024-04-03 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 55–713(659 aa)
Not recorded A1AKL N-{5-[(piperidin-1-yl)methyl]-1,3-thiazol-2-yl}acetamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 8.5;281 K;33% PEG 300, 100mM Hepes pH 8.5
Resolution 2.75 Å R-free 0.260
9NE2 cryoEM structure of the human OGA-L Catalytic Dimer Deposited 2025-02-19 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–916(916 aa)
Chain B 1–916(916 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.63 Å
9NE4 cryoEM structure of the A-chain of the human OGA-L Catalytic Dimer Deposited 2025-02-19 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–916(916 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.98 Å
9NE5 cryoEM structure of the B-chain of the human OGA-L Catalytic Dimer Deposited 2025-02-19 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain B 1–916(916 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.05 Å
9QEN Cryo-EM structure of human O-GlcNAcase Deposited 2025-03-10 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 11–420(410 aa)
Chain A 553–916(364 aa)
Chain B 11–420(410 aa)
Chain B 553–916(364 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.08 Å