2JCJ

Crystal structure of alpha-1,3 Galactosyltransferase (C-terminus truncated mutant-C3) in complex with UDP and Tris

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005975	biological_process	carbohydrate metabolic process
A	0016020	cellular_component	membrane
A	0016758	molecular_function	hexosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A1367

Chain	Residue
A	ASP225
A	ASP227
A	UDP1366
A	HOH2200

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site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE UDP A1366

Chain	Residue
A	TYR139
A	ILE198
A	SER199
A	ARG202
A	ASP225
A	VAL226
A	ASP227
A	GLU360
A	MN1367
A	TRS1369
A	HOH2097
A	HOH2199
A	HOH2201
A	LYS102
A	LYS104
A	PHE134
A	ALA135
A	VAL136

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TRS A1369

Chain	Residue
A	LYS104
A	GLN247
A	TYR278
A	HIS280
A	GLU317
A	TRP356
A	GLU360
A	UDP1366
A	HOH2125
A	HOH2201
A	HOH2202

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD A1368

Chain	Residue
A	TYR341
A	ILE349
A	LYS350
A	LEU351
A	VAL352
A	HOH2189

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A1370

Chain	Residue
A	PRO174
A	LEU175
A	ILE176
A	PHE184
A	HOH2203

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:11179209, ECO:0007744|PDB:1G8O

Chain	Residue	Details
A	GLU317

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:11179209, ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1G93, ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GWW, ECO:0007744|PDB:1GX0, ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1K4V, ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZT, ECO:0007744|PDB:1VZU, ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2JCK, ECO:0007744|PDB:2VFZ, ECO:0007744|PDB:2VS3, ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2VS5, ECO:0007744|PDB:2VXL, ECO:0007744|PDB:2WGZ

Chain	Residue	Details
A	PHE134

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:11179209, ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1G8O, ECO:0007744|PDB:1G93, ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GWW, ECO:0007744|PDB:1GX0, ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1K4V, ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZT, ECO:0007744|PDB:1VZU, ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2JCK, ECO:0007744|PDB:2VFZ, ECO:0007744|PDB:2VS3, ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2VS5, ECO:0007744|PDB:2VXL, ECO:0007744|PDB:2WGZ

Chain	Residue	Details
A	ASP227
A	ASP225

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2WGZ

Chain	Residue	Details
A	THR259
A	GLN247

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GWW, ECO:0007744|PDB:1GX0, ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1K4V, ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZT, ECO:0007744|PDB:1VZU, ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2JCK, ECO:0007744|PDB:2VFZ, ECO:0007744|PDB:2VS3, ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2VS5, ECO:0007744|PDB:2WGZ

Chain	Residue	Details
A	LYS359

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN293

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 356

Chain	Residue	Details
A	GLN247	electrostatic stabiliser, hydrogen bond donor
A	HIS280	electrostatic stabiliser, hydrogen bond donor
A	TRP314	electrostatic stabiliser, hydrogen bond donor
A	GLU317	activator, covalently attached, electrostatic stabiliser, nucleofuge, nucleophile
A	TRP356	electrostatic stabiliser, hydrogen bond donor
A	ARG365	electrostatic stabiliser

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