4NV1

Crystal structure of a 4-N formyltransferase from Francisella tularensis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0009058	biological_process	biosynthetic process
A	0016740	molecular_function	transferase activity
B	0009058	biological_process	biosynthetic process
B	0016740	molecular_function	transferase activity
C	0009058	biological_process	biosynthetic process
C	0016740	molecular_function	transferase activity
D	0009058	biological_process	biosynthetic process
D	0016740	molecular_function	transferase activity
E	0009058	biological_process	biosynthetic process
E	0016740	molecular_function	transferase activity
F	0009058	biological_process	biosynthetic process
F	0016740	molecular_function	transferase activity
G	0009058	biological_process	biosynthetic process
G	0016740	molecular_function	transferase activity
H	0009058	biological_process	biosynthetic process
H	0016740	molecular_function	transferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 0FX C 301

Chain	Residue
C	ASN10
C	TYR218
C	ASN220
C	HOH494
C	HIS73
C	SER74
C	LYS75
C	TRP102
C	PHE103
C	GLN105
C	TYR149
C	HIS215

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 302

Chain	Residue
C	ASP225
C	GLU226
C	HOH481
D	ARG204

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site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TYD D 301

Chain	Residue
D	ASN10
D	HIS73
D	PHE103
D	GLN105
D	TYR149
D	HIS215
D	TYR218
D	ASN220

---

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 0FX E 301

Chain	Residue
E	ASN10
E	HIS73
E	LYS75
E	PHE103
E	GLN105
E	TYR149
E	HIS215
E	TYR218
E	ASN220
E	HOH402
E	HOH417
E	HOH438
E	HOH478
E	HOH486

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site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TYD F 301

Chain	Residue
F	ASN10
F	HIS73
F	PHE103
F	GLN105
F	TYR149
F	HIS215
F	TYR218
F	ASN220

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 F 302

Chain	Residue
E	ASP225
E	GLU226
F	ARG204

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site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 4TG B 301

Chain	Residue
B	ASN10
B	HIS73
B	SER74
B	LYS75
B	TRP102
B	PHE103
B	GLN105
B	TYR149
B	HIS215
B	TYR218
B	ASN220
B	HOH414
B	HOH437
B	HOH445

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 302

Chain	Residue
A	ARG204
B	ASP225
B	GLU226
B	HOH468

---

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 0FX A 301

Chain	Residue
A	ASN10
A	HIS73
A	LYS75
A	PHE103
A	GLN105
A	TYR149
A	HIS215
A	TYR218
A	ASN220
A	HOH452
A	HOH477
A	HOH515

---

site_id	BC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 0FX G 301

Chain	Residue
G	ASN10
G	HIS73
G	LYS75
G	TRP102
G	PHE103
G	GLN105
G	TYR149
G	TYR189
G	HIS215
G	TYR218
G	ASN220
G	HOH418

---

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TYD H 301

Chain	Residue
H	HOH439
H	HOH464
H	HIS73
H	PHE103
H	GLN105
H	TYR149
H	HIS215
H	TYR218
H	ASN220
H	HOH428

---

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 H 302

Chain	Residue
G	ARG204
H	LEU197
H	ASP225
H	GLU226
H	HOH497

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site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 H 303

Chain	Residue
G	ASP225
G	GLU226
H	ARG204

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Functional Information from PROSITE/UniProt

site_id	PS00373
Number of Residues	24
Details	GART Phosphoribosylglycinamide formyltransferase active site. GaTIhVMdEeIDhGdiIiqeeveV

Chain	Residue	Details
C	GLY116-VAL139

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