Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1CDE

STRUCTURES OF APO AND COMPLEXED ESCHERICHIA COLI GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004644	molecular_function	phosphoribosylglycinamide formyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0006189	biological_process	'de novo' IMP biosynthetic process
A	0006974	biological_process	DNA damage response
A	0009058	biological_process	biosynthetic process
A	0016740	molecular_function	transferase activity
B	0003824	molecular_function	catalytic activity
B	0004644	molecular_function	phosphoribosylglycinamide formyltransferase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0006189	biological_process	'de novo' IMP biosynthetic process
B	0006974	biological_process	DNA damage response
B	0009058	biological_process	biosynthetic process
B	0016740	molecular_function	transferase activity
C	0003824	molecular_function	catalytic activity
C	0004644	molecular_function	phosphoribosylglycinamide formyltransferase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006164	biological_process	purine nucleotide biosynthetic process
C	0006189	biological_process	'de novo' IMP biosynthetic process
C	0006974	biological_process	DNA damage response
C	0009058	biological_process	biosynthetic process
C	0016740	molecular_function	transferase activity
D	0003824	molecular_function	catalytic activity
D	0004644	molecular_function	phosphoribosylglycinamide formyltransferase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006164	biological_process	purine nucleotide biosynthetic process
D	0006189	biological_process	'de novo' IMP biosynthetic process
D	0006974	biological_process	DNA damage response
D	0009058	biological_process	biosynthetic process
D	0016740	molecular_function	transferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GAR A 222

Chain	Residue
A	ASN10
A	GLN170
A	GLU173
A	DZF225
A	GLY11
A	SER12
A	ASN13
A	GLY87
A	MET89
A	ILE107
A	HIS108
A	PRO109

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE DZF A 225

Chain	Residue
A	MET89
A	ARG90
A	ILE91
A	LEU92
A	VAL97
A	ASN106
A	VAL139
A	THR140
A	ASP141
A	GLU142
A	ASP144
A	GAR222

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GAR B 222

Chain	Residue
B	ASN10
B	GLY11
B	SER12
B	ASN13
B	GLY87
B	MET89
B	ILE107
B	HIS108
B	PRO109
B	GLN170
B	GLU173
B	DZF225

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE DZF B 225

Chain	Residue
B	MET89
B	ARG90
B	ILE91
B	LEU92
B	VAL97
B	ASN106
B	VAL139
B	THR140
B	ASP141
B	GLU142
B	ASP144
B	GAR222

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GAR C 222

Chain	Residue
C	ASN10
C	GLY11
C	SER12
C	ASN13
C	GLY87
C	MET89
C	ILE107
C	HIS108
C	PRO109
C	GLN170
C	GLU173
C	DZF225

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE DZF C 225

Chain	Residue
C	MET89
C	ARG90
C	ILE91
C	LEU92
C	VAL97
C	ASN106
C	VAL139
C	THR140
C	ASP141
C	GLU142
C	ASP144
C	GAR222

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GAR D 222

Chain	Residue
D	ASN10
D	GLY11
D	SER12
D	ASN13
D	GLY87
D	MET89
D	ILE107
D	HIS108
D	PRO109
D	GLN170
D	GLU173
D	DZF225

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE DZF D 225

Chain	Residue
D	MET89
D	ARG90
D	ILE91
D	LEU92
D	VAL97
D	ASN106
D	VAL139
D	THR140
D	ASP141
D	GLU142
D	ASP144
D	GAR222

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY133-VAL156

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01930","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10433709","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01930","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10606510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1631098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01930","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10606510","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10606510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1631098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Site: {"description":"Raises pKa of active site His","evidences":[{"source":"HAMAP-Rule","id":"MF_01930","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10433709","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 1631098

Chain	Residue	Details
A	ASN106
A	ASP144
A	HIS108

site_id	CSA2
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 1631098

Chain	Residue	Details
B	ASN106
B	ASP144
B	HIS108

site_id	CSA3
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 1631098

Chain	Residue	Details
C	ASN106
C	ASP144
C	HIS108

site_id	CSA4
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 1631098

Chain	Residue	Details
D	ASN106
D	ASP144
D	HIS108

site_id	MCSA1
Number of Residues	4
Details	M-CSA 363

Chain	Residue	Details
A	ASN106	electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
A	HIS108	activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
A	SER135	electrostatic stabiliser, hydrogen bond donor, steric role
A	ASP144	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, increase electrophilicity

site_id	MCSA2
Number of Residues	4
Details	M-CSA 363

Chain	Residue	Details
B	ASN106	electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
B	HIS108	activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
B	SER135	electrostatic stabiliser, hydrogen bond donor, steric role
B	ASP144	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, increase electrophilicity

site_id	MCSA3
Number of Residues	4
Details	M-CSA 363

Chain	Residue	Details
C	ASN106	electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
C	HIS108	activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
C	SER135	electrostatic stabiliser, hydrogen bond donor, steric role
C	ASP144	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, increase electrophilicity

site_id	MCSA4
Number of Residues	4
Details	M-CSA 363

Chain	Residue	Details
D	ASN106	electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
D	HIS108	activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
D	SER135	electrostatic stabiliser, hydrogen bond donor, steric role
D	ASP144	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, increase electrophilicity

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)