6Z2F

Crystal structure of human AGX1 mutant complexed with UDPGLCNAC

Functional Information from GO Data

Chain	GOid	namespace	contents
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	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	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	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	21
Details	binding site for residue UD1 A 601

Chain	Residue
A	LEU108
A	GLY290
A	GLU303
A	TYR304
A	ASN327
A	PHE381
A	PHE383
A	PHE403
A	LYS407
A	HOH860
A	HOH887
A	MET165
A	HOH919
B	LYS455
A	GLN196
A	PRO220
A	GLY222
A	ASN223
A	CYS251
A	VAL252
A	VAL289

---

site_id	AC2
Number of Residues	26
Details	binding site for residue UD1 B 601

Chain	Residue
A	ARG453
B	GLY110
B	GLY111
B	GLN112
B	GLY113
B	THR114
B	ARG115
B	LYS122
B	ASN223
B	YCM251
B	VAL289
B	GLY290
B	GLU303
B	TYR304
B	ASN327
B	PHE381
B	PHE383
B	LYS407
B	HOH712
B	HOH719
B	HOH745
B	HOH750
B	HOH751
B	HOH753
B	HOH768
B	HOH953

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	11
Details	BINDING: BINDING => ECO:0000269|PubMed:11707391, ECO:0007744|PDB:1JV1, ECO:0007744|PDB:1JVD

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

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:11707391, ECO:0007744|PDB:1JV1

Chain	Residue	Details
B	YCM251
B	TYR472

---

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

Chain	Residue	Details
B	PHE381

---

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

Chain	Residue	Details
B	LYS407

---