5NPR

The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006493	biological_process	protein O-linked glycosylation
A	0016757	molecular_function	glycosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue K A 1101

Chain	Residue
A	HOH1209
A	HOH1325
A	HOH1325
A	HOH1347
A	HOH1513
A	HOH1554
A	HOH1556

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site_id	AC2
Number of Residues	22
Details	binding site for residue 94T E 101

Chain	Residue
A	GLN839
A	LYS842
A	LEU866
A	VAL895
A	ALA896
A	LYS898
A	HIS901
A	ARG904
A	HIS920
A	THR921
A	THR922
A	ASP925
A	HOH1320
E	THR3
E	PRO4
E	VAL5
E	CYS6
E	HOH202
E	HOH204
E	HOH206
A	PRO559
A	ASN838

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:21240259, ECO:0000305|PubMed:26678539

Chain	Residue	Details
A	HIS498

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:23103939, ECO:0007744|PDB:4GYW

Chain	Residue	Details
A	GLN839
A	LYS842
A	ALA896
A	HIS901
A	HIS920
A	ASP925

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by AMPK => ECO:0000269|PubMed:24563466, ECO:0000269|PubMed:37541260

Chain	Residue	Details
A	THR444

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P56558

Chain	Residue	Details
A	TYR979

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site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: O-linked (GlcNAc) serine; by autocatalysis => ECO:0000269|PubMed:27713473

Chain	Residue	Details
A	SER389

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