1JBW

FPGS-AMPPCP-folate complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004326	molecular_function	tetrahydrofolylpolyglutamate synthase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006730	biological_process	one-carbon metabolic process
A	0006761	biological_process	dihydrofolate biosynthetic process
A	0008841	molecular_function	dihydrofolate synthase activity
A	0009058	biological_process	biosynthetic process
A	0009396	biological_process	folic acid-containing compound biosynthetic process
A	0016874	molecular_function	ligase activity
A	0016881	molecular_function	acid-amino acid ligase activity
A	0046872	molecular_function	metal ion binding
A	0046901	biological_process	tetrahydrofolylpolyglutamate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 997

Chain	Residue
A	HOH432
A	HOH433
A	HOH434
A	HOH435
A	HOH795
A	ACQ999

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 998

Chain	Residue
A	HOH431
A	ACQ999
A	SER73
A	GLU143
A	HOH430

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site_id	AC3
Number of Residues	33
Details	BINDING SITE FOR RESIDUE ACQ A 999

Chain	Residue
A	THR47
A	ASN48
A	GLY49
A	LYS50
A	GLY51
A	SER52
A	SER73
A	GLU143
A	GLU165
A	TYR260
A	ASN264
A	TRP297
A	ARG300
A	ASP313
A	GLY314
A	ALA315
A	HIS316
A	ASP319
A	SER412
A	LEU413
A	TYR414
A	HOH431
A	HOH432
A	HOH434
A	HOH466
A	HOH498
A	HOH549
A	HOH553
A	HOH736
A	HOH795
A	HOH815
A	MG997
A	MG998

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site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE TMF A 996

Chain	Residue
A	ARG15
A	PRO74
A	PHE75
A	ARG82
A	GLU120
A	PHE121
A	TYR414
A	SER417
A	HOH514
A	HOH536
A	HOH564
A	HOH637

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Functional Information from PROSITE/UniProt

site_id	PS01011
Number of Residues	24
Details	FOLYLPOLYGLU_SYNT_1 Folylpolyglutamate synthase signature 1. IhVTGTNGKgSaanaIaHVLeas.G

Chain	Residue	Details
A	ILE42-GLY65

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site_id	PS01012
Number of Residues	16
Details	FOLYLPOLYGLU_SYNT_2 Folylpolyglutamate synthase signature 2. VIEvGIGGdtDsTnVI

Chain	Residue	Details
A	VAL141-ILE156

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:11501996, ECO:0007744|PDB:1JBV, ECO:0007744|PDB:1JBW

Chain	Residue	Details
A	GLY49
A	ARG300
A	ASP313

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:11501996, ECO:0007744|PDB:1JBV, ECO:0007744|PDB:1JBW

Chain	Residue	Details
A	SER73
A	GLU143

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:11501996, ECO:0007744|PDB:1JBW

Chain	Residue	Details
A	PHE75
A	ARG82
A	ASN264
A	SER417

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:11501996, ECO:0007744|PDB:1JBV

Chain	Residue	Details
A	HIS170

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:11501996, ECO:0007744|PDB:1JBV, ECO:0007744|PDB:1JBW

Chain	Residue	Details
A	KCX185

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1p3d

Chain	Residue	Details
A	LYS50

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