Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1JKX

Unexpected formation of an epoxide-derived multisubstrate adduct inhibitor on the active site of GAR 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	33
Details	BINDING SITE FOR RESIDUE 138 A 1221

Chain	Residue
A	ASN10
A	ILE91
A	LEU92
A	VAL97
A	ILE107
A	HIS108
A	PRO109
A	VAL139
A	GLN170
A	GLU173
A	HOH1222
A	GLY11
A	HOH1223
A	HOH1230
A	HOH1233
A	HOH1236
A	HOH1238
A	HOH1240
A	HOH1241
A	HOH1242
A	HOH1308
A	HOH1320
A	SER12
A	HOH1330
A	HOH1344
A	HOH1387
C	LYS153
A	ASN13
A	ARG64
A	GLY87
A	PHE88
A	MET89
A	ARG90

site_id	AC2
Number of Residues	33
Details	BINDING SITE FOR RESIDUE 138 B 2221

Chain	Residue
B	ASN10
B	GLY11
B	SER12
B	ASN13
B	LYS37
B	ARG64
B	GLY87
B	PHE88
B	MET89
B	ARG90
B	ILE91
B	LEU92
B	VAL97
B	ILE107
B	HIS108
B	PRO109
B	VAL139
B	GLU173
B	HOH2227
B	HOH2231
B	HOH2233
B	HOH2240
B	HOH2246
B	HOH2251
B	HOH2255
B	HOH2266
B	HOH2278
B	HOH2288
B	HOH2307
B	HOH2342
B	HOH2384
D	GLU131
D	LYS153

site_id	AC3
Number of Residues	31
Details	BINDING SITE FOR RESIDUE 138 C 3221

Chain	Residue
C	ASN10
C	GLY11
C	SER12
C	ASN13
C	ARG64
C	GLY87
C	PHE88
C	MET89
C	ARG90
C	ILE91
C	LEU92
C	VAL97
C	ILE107
C	HIS108
C	PRO109
C	VAL139
C	GLN170
C	GLU173
C	HOH3224
C	HOH3234
C	HOH3248
C	HOH3259
C	HOH3266
C	HOH3270
C	HOH3280
C	HOH3286
C	HOH3292
C	HOH3319
C	HOH3339
C	HOH3365
C	HOH3366

site_id	AC4
Number of Residues	29
Details	BINDING SITE FOR RESIDUE 138 D 4221

Chain	Residue
D	GLY11
D	SER12
D	ASN13
D	ARG64
D	GLY87
D	PHE88
D	MET89
D	ARG90
D	ILE91
D	LEU92
D	VAL97
D	ILE107
D	HIS108
D	PRO109
D	VAL139
D	GLU173
D	HOH4224
D	HOH4227
D	HOH4230
D	HOH4237
D	HOH4261
D	HOH4262
D	HOH4277
D	HOH4283
D	HOH4326
D	HOH4327
D	HOH4328
B	GLU131
D	ASN10

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	4
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
A	SER135
A	ASN106
A	ASP144
A	HIS108

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
B	ASP144
B	HIS108

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
C	ASP144
C	HIS108

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
D	ASP144
D	HIS108

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

Chain	Residue	Details
B	SER135
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	SER135
C	ASN106
C	ASP144
C	HIS108

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
D	SER135
D	ASN106
D	ASP144
D	HIS108

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

Chain	Residue	Details
A	ASN106
A	ASP144
A	HIS108

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

Chain	Residue	Details
B	ASN106
B	ASP144
B	HIS108

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
C	ASN106
C	ASP144
C	HIS108

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1c2t

Chain	Residue	Details
D	ASN106
D	ASP144
D	HIS108

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

Chain	Residue	Details
A	ASP144
A	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)