7OU6: Human O-GlcNAc hydrolase

Name: PDB 7OU6: Human O-GlcNAc hydrolase in complex with DNJNAc-thiazolidines
Published: 2022-04-13
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: hydrolase

Human O-GlcNAc hydrolase in complex with DNJNAc-thiazolidines. Determined by X-ray diffraction at 2.41 Å resolution. Released 13 Apr 2022.

Method: X-ray diffraction
Resolution: 2.41 Å
Organism: Homo sapiens
Chains: 2
Atoms: 6,768
Mol. weight: 206.71 kDa
Ligands: 1XI
Released: 13 Apr 2022

Explore 7OU6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7OU6 contains 47 α-helices and 18 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 AAA: 23 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	61-66	6	1
α-helix	72-74	3
α-helix	75-88	14
β-strand	92-95	4	1
α-helix	101-103	3
α-helix	110-111	2
α-helix	113-127	15
β-strand	132-137	6	1
α-helix	148-163	16
β-strand	168-172	5	1
α-helix	182-187	6
α-helix	191-205	15
β-strand	212-215	4	1
α-helix	232-240	9
β-strand	246-249	4	1
α-helix	261-271	11
α-helix	274-275	2
β-strand	276-279	4	1
α-helix	295-296	2
α-helix	301-306	6
β-strand	309-312	4	1
α-helix	318-320	3
α-helix	321-333	13
α-helix	376-387	12
α-helix	545-547	3
α-helix	552-553	2
α-helix	555-564	10
α-helix	573-587	15
α-helix	614-628	15
α-helix	634-657	24
α-helix	684-690	7

Chain BBB: 24 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	61-66	6	2
α-helix	72-74	3
α-helix	75-88	14
β-strand	92-95	4	2
α-helix	101-103	3
α-helix	110-112	3
α-helix	113-128	16
β-strand	132-137	6	2
α-helix	148-163	16
β-strand	168-172	5	2
α-helix	182-187	6
α-helix	191-205	15
β-strand	212-215	4	2
α-helix	221-223	3
α-helix	232-240	9
β-strand	246-249	4	2
α-helix	261-271	11
β-strand	276-279	4	2
α-helix	295-296	2
α-helix	301-306	6
β-strand	309-312	4	2
α-helix	318-321	4
α-helix	322-333	12
α-helix	376-388	13
α-helix	389-392	4
α-helix	545-546	2
α-helix	552-553	2
α-helix	555-564	10
β-strand	567	1	3
β-strand	570	1	3
α-helix	573-587	15
α-helix	604-628	25
α-helix	634-661	28
α-helix	684-690	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein O-GlcNAcase	AAA, BBB	protein	916	Homo sapiens	O60502 (AlphaFold model)

Sequence of entity 1 (AAA, BBB), FASTA

>7OU6_1 Protein O-GlcNAcase (chains AAA, BBB)
MVQKESQATLEERESELSSNPAASAGASLEPPAAPAPGEDNPAGAGGAAVAGAAGGARRF
LCGVVEGFYGRPWVMEQRKELFRRLQKWELNTYLYAPKDDYKHRMFWREMYSVEEAEQLM
TLISAAREYEIEFIYAISPGLDITFSNPKEVSTLKRKLDQVSQFGCRSFALLFDDIDHNM
CAADKEVFSSFAHAQVSITNEIYQYLGEPETFLFCPTEYCGTFCYPNVSQSPYLRTVGEK
LLPGIEVLWTGPKVVSKEIPVESIEEVSKIIKRAPVIWDNIHANDYDQKRLFLGPYKGRS
TELIPRLKGVLTNPNCEFEANYVAIHTLATWYKSNMNGVRKDVVMTDSEDSTVSIQIKLE
NEGSDEDIETDVLYSPQMALKLALTEWLQEFGVPHQYSSRQVAHSGAKASVVDGTPLVAA
PSLNATTVVTTVYQEPIMSQGAALSGEPTTLTKEEEKKQPDEEPMDMVVEKQEETDHKND
NQILSEIVEAKMAEELKPMDTDKESIAESKSPEMSMQEDCISDIAPMQTDEQTNKEQFVP
GPNEKPLYTAEPVTLEDLQLLADLFYLPYEHGPKGAQMLREFQWLRANSSVVSVNCKGKD
SEKIEEWRSRAAKFEEMCGLVMGMFTRLSNCANRTILYDMYSYVWDIKSIMSMVKSFVQW
LGCRSHSSAQFLIGDQEPWAFRGGLAGEFQRLLPIDGANDLFFQPPPLTPTSKVYTIRPY
FPKDEASVYKICREMYDDGVGLPFQSQPDLIGDKLVGGLLSLSLDYCFVLEDEDGICGYA
LGTVDVTPFIKKCKISWIPFMQEKYTKPNGDKELSEAEKIMLSFHEEQEVLPETFLANFP
SLIKMDIHKKVTDPSVAKSMMACLLSSLKANGSRGAFCEVRPDDKRILEFYSKLGCFEIA
KMEGFPKDVVILGRSL

Ligands and cofactors

ID	Name	Formula	Copies
1XI	~{N}-[(3~{Z},6~{S},7~{R},8~{R},8~{a}~{S})-7,8-bis(oxidanyl)-3-(phenylmethyl)imi…	C16 H21 N3 O3 S	2

Primary citation

Bicyclic Picomolar OGA Inhibitors Enable Chemoproteomic Mapping of Its Endogenous Post-translational Modifications. Gonzalez-Cuesta, M., Sidhu, P., Ashmus, R.A. et al. J Am Chem Soc (2022) 144:832-844. DOI 10.1021/jacs.1c10504

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
11LJ 2.33 Å, Human oga in complex with ligand 24
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
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

Browse structure collections

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