2AM3

Crystal Structure of N-Acetylglucosaminyltransferase I in Complex with UDP-Glucose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006486	biological_process	protein glycosylation
A	0008375	molecular_function	acetylglucosaminyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 448

Chain	Residue
A	ASP213
A	UPG449
A	HOH489
A	HOH533
A	HOH554

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site_id	AC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE UPG A 449

Chain	Residue
A	ASP144
A	CYS145
A	TYR184
A	LYS186
A	ILE187
A	HIS190
A	GLU211
A	ASP212
A	ASP213
A	TRP290
A	ASP291
A	GLY320
A	VAL321
A	SER322
A	MN448
A	GOL450
A	HOH457
A	HOH479
A	HOH489
A	HOH491
A	HOH519
A	HOH617
A	ILE113
A	ALA114
A	CYS115
A	ARG117

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 450

Chain	Residue
A	TYR184
A	PHE289
A	ASP291
A	ASP292
A	UPG449

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site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 451

Chain	Residue
A	ARG131
A	ILE139
A	SER159
A	ALA160
A	THR162

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site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 452

Chain	Residue
A	TYR390
A	GLY412
A	GLY420
A	TRP439
A	GLY441
A	TYR442
A	ASP443
A	TRP446

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site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 453

Chain	Residue
A	PRO235
A	LEU237
A	LEU274
A	ARG303
A	HOH483
A	HOH506

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255

Chain	Residue	Details
A	ASP291

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:11032794, ECO:0000269|PubMed:16769084, ECO:0007744|PDB:1FOA, ECO:0007744|PDB:2AM3, ECO:0007744|PDB:2AM4, ECO:0007744|PDB:2AM5, ECO:0007744|PDB:2APC

Chain	Residue	Details
A	ARG117
A	ASP144
A	HIS190
A	ASP212

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:11032794, ECO:0007744|PDB:1FOA

Chain	Residue	Details
A	ASP213

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:11032794, ECO:0000269|PubMed:16769084, ECO:0007744|PDB:1FOA, ECO:0007744|PDB:2AM3, ECO:0007744|PDB:2AM4, ECO:0007744|PDB:2AM5

Chain	Residue	Details
A	SER322

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1foa

Chain	Residue	Details
A	ASP291

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site_id	MCSA1
Number of Residues	2
Details	M-CSA 770

Chain	Residue	Details
A	ASP213	metal ligand
A	ASP291	activator, proton acceptor, proton donor

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