4EW1

High resolution structure of human glycinamide ribonucleotide transformylase in apo form.

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 301

Chain	Residue
A	GLY11
A	ASN13
A	LEU14
A	GLN15
A	ALA16
A	LYS45
A	HIS174
A	HOH477
A	HOH487

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 302

Chain	Residue
A	LYS157
A	ARG168
A	HOH429
A	HOH617

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 303

Chain	Residue
A	PRO109
A	HIS121
A	LYS170
A	HOH407
A	HOH475
A	HOH585

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site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 304

Chain	Residue
A	ASN119
A	ALA120
A	HIS121
A	GLU122
A	VAL162
A	SER166
A	HOH585

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P08179

Chain	Residue	Details
A	HIS108

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site_id	SWS_FT_FI2
Number of Residues	2
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

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:12755606, ECO:0007744|PDB:1NJS

Chain	Residue	Details
A	ARG64
A	ASN106

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site_id	SWS_FT_FI4
Number of Residues	2
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

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Raises pKa of active site His => ECO:0000250|UniProtKB:P08179

Chain	Residue	Details
A	ASP144

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