1MEN

complex structure of human GAR Tfase and substrate beta-GAR

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004644	molecular_function	phosphoribosylglycinamide formyltransferase activity
A	0006189	biological_process	'de novo' IMP biosynthetic process
A	0009058	biological_process	biosynthetic process
B	0004644	molecular_function	phosphoribosylglycinamide formyltransferase activity
B	0006189	biological_process	'de novo' IMP biosynthetic process
B	0009058	biological_process	biosynthetic process
C	0004644	molecular_function	phosphoribosylglycinamide formyltransferase activity
C	0006189	biological_process	'de novo' IMP biosynthetic process
C	0009058	biological_process	biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GAR A 223

Chain	Residue
A	THR10
A	HOH231
A	HOH235
A	HOH264
A	GLY11
A	SER12
A	ASN13
A	MET89
A	PRO109
A	LYS170
A	GLU173
A	HOH225

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE GAR B 224

Chain	Residue
B	THR10
B	GLY11
B	SER12
B	ASN13
B	GLY87
B	MET89
B	PRO109
B	LYS170
B	GLU173
B	HOH225
B	HOH226
B	HOH229
B	HOH235
B	HOH239
B	HOH244

---

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE GAR C 225

Chain	Residue
C	THR10
C	GLY11
C	SER12
C	ASN13
C	GLY87
C	MET89
C	ILE107
C	PRO109
C	LYS170
C	GLU173
C	HOH226
C	HOH232
C	HOH233
C	HOH241
C	HOH251

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY133-VAL156

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P08179

Chain	Residue	Details
A	HIS108
B	HIS108
C	HIS108

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:12450384, ECO:0000269|PubMed:16026156, ECO:0007744|PDB:1MEN, ECO:0007744|PDB:1ZLY

Chain	Residue	Details
A	GLY11
A	LYS170
B	GLY11
B	LYS170
C	GLY11
C	LYS170

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305|PubMed:12755606, ECO:0007744|PDB:1NJS

Chain	Residue	Details
A	ARG64
A	ASN106
B	ARG64
B	ASN106
C	ARG64
C	ASN106

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305|PubMed:12755606, ECO:0000305|PubMed:16026156, ECO:0007744|PDB:1NJS, ECO:0007744|PDB:1ZLY

Chain	Residue	Details
A	MET89
A	ALA140
B	MET89
B	ALA140
C	MET89
C	ALA140

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	SITE: Raises pKa of active site His => ECO:0000250|UniProtKB:P08179

Chain	Residue	Details
A	ASP144
B	ASP144
C	ASP144

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
A	THR135
A	ASN106
A	ASP144
A	HIS108

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
B	THR135
B	ASN106
B	ASP144
B	HIS108

---

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
C	THR135
C	ASN106
C	ASP144
C	HIS108

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
A	ASN106
A	ASP144
A	HIS108

---

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
B	ASN106
B	ASP144
B	HIS108

---

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
C	ASN106
C	ASP144
C	HIS108

---

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
A	ASP144
A	HIS108

---

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
B	ASP144
B	HIS108

---

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
C	ASP144
C	HIS108

---