1JVD

CRYSTAL STRUCTURE OF HUMAN AGX2 COMPLEXED WITH UDPGLCNAC

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002376	biological_process	immune system process
A	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
A	0016779	molecular_function	nucleotidyltransferase activity
A	0032481	biological_process	positive regulation of type I interferon production
A	0042802	molecular_function	identical protein binding
A	0045087	biological_process	innate immune response
A	0052630	molecular_function	UDP-N-acetylgalactosamine diphosphorylase activity
A	0070569	molecular_function	uridylyltransferase activity
A	0140374	biological_process	antiviral innate immune response
A	0141090	molecular_function	protein serine pyrophosphorylase activity
B	0002376	biological_process	immune system process
B	0003977	molecular_function	UDP-N-acetylglucosamine diphosphorylase activity
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
B	0016779	molecular_function	nucleotidyltransferase activity
B	0032481	biological_process	positive regulation of type I interferon production
B	0042802	molecular_function	identical protein binding
B	0045087	biological_process	innate immune response
B	0052630	molecular_function	UDP-N-acetylgalactosamine diphosphorylase activity
B	0070569	molecular_function	uridylyltransferase activity
B	0140374	biological_process	antiviral innate immune response
B	0141090	molecular_function	protein serine pyrophosphorylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE UD1 A 901

Chain	Residue
A	LEU108
A	VAL252
A	VAL289
A	GLY290
A	GLU303
A	TYR304
A	ASN327
A	PHE381
A	PHE383
A	PHE403
A	LYS407
A	ALA109
A	HOH931
A	HOH972
A	HOH1020
B	ARG453
A	GLY110
A	MET165
A	GLN196
A	PRO220
A	GLY222
A	ASN223
A	CYS251

---

site_id	AC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE UD1 B 902

Chain	Residue
A	ARG453
B	LEU108
B	ALA109
B	GLY110
B	GLY111
B	MET165
B	GLN196
B	PRO220
B	GLY222
B	ASN223
B	CYS251
B	VAL252
B	VAL289
B	GLY290
B	GLU303
B	TYR304
B	ASN327
B	PHE381
B	PHE383
B	PHE403
B	LYS407
B	HOH916
B	HOH939
B	HOH1019

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	22
Details	BINDING: BINDING => ECO:0000269|PubMed:11707391, ECO:0007744|PDB:1JV1, ECO:0007744|PDB:1JVD

Chain	Residue	Details
A	LEU108
A	TYR304
A	ASN327
B	LEU108
B	GLY110
B	GLY111
B	GLN196
B	GLY222
B	ASN223
B	VAL252
B	GLY290
A	GLY110
B	GLU303
B	TYR304
B	ASN327
A	GLY111
A	GLN196
A	GLY222
A	ASN223
A	VAL252
A	GLY290
A	GLU303

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:11707391, ECO:0007744|PDB:1JV1

Chain	Residue	Details
A	CYS251
A	LYS472
B	CYS251
B	LYS472

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:11707391, ECO:0007744|PDB:1JVD

Chain	Residue	Details
A	PHE381
B	PHE381

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0007744|PDB:1JV1, ECO:0007744|PDB:1JVD

Chain	Residue	Details
A	LYS407
B	LYS407

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