Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3RG2

Structure of a two-domain NRPS fusion protein containing the EntE adenylation domain and EntB aryl-carrier protein from enterobactin biosynthesis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0008668	molecular_function	2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
A	0009239	biological_process	enterobactin biosynthetic process
A	0016020	cellular_component	membrane
A	0016746	molecular_function	acyltransferase activity
A	0016874	molecular_function	ligase activity
A	0016877	molecular_function	ligase activity, forming carbon-sulfur bonds
A	0019290	biological_process	siderophore biosynthetic process
A	0047527	molecular_function	2,3-dihydroxybenzoate-serine ligase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005829	cellular_component	cytosol
B	0008668	molecular_function	2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
B	0009239	biological_process	enterobactin biosynthetic process
B	0016020	cellular_component	membrane
B	0016746	molecular_function	acyltransferase activity
B	0016874	molecular_function	ligase activity
B	0016877	molecular_function	ligase activity, forming carbon-sulfur bonds
B	0019290	biological_process	siderophore biosynthetic process
B	0047527	molecular_function	2,3-dihydroxybenzoate-serine ligase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005829	cellular_component	cytosol
C	0008668	molecular_function	2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
C	0009239	biological_process	enterobactin biosynthetic process
C	0016020	cellular_component	membrane
C	0016746	molecular_function	acyltransferase activity
C	0016874	molecular_function	ligase activity
C	0016877	molecular_function	ligase activity, forming carbon-sulfur bonds
C	0019290	biological_process	siderophore biosynthetic process
C	0047527	molecular_function	2,3-dihydroxybenzoate-serine ligase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005829	cellular_component	cytosol
D	0008668	molecular_function	2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
D	0009239	biological_process	enterobactin biosynthetic process
D	0016020	cellular_component	membrane
D	0016746	molecular_function	acyltransferase activity
D	0016874	molecular_function	ligase activity
D	0016877	molecular_function	ligase activity, forming carbon-sulfur bonds
D	0019290	biological_process	siderophore biosynthetic process
D	0047527	molecular_function	2,3-dihydroxybenzoate-serine ligase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005829	cellular_component	cytosol
E	0008668	molecular_function	2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
E	0009239	biological_process	enterobactin biosynthetic process
E	0016020	cellular_component	membrane
E	0016746	molecular_function	acyltransferase activity
E	0016874	molecular_function	ligase activity
E	0016877	molecular_function	ligase activity, forming carbon-sulfur bonds
E	0019290	biological_process	siderophore biosynthetic process
E	0047527	molecular_function	2,3-dihydroxybenzoate-serine ligase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005829	cellular_component	cytosol
F	0008668	molecular_function	2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
F	0009239	biological_process	enterobactin biosynthetic process
F	0016020	cellular_component	membrane
F	0016746	molecular_function	acyltransferase activity
F	0016874	molecular_function	ligase activity
F	0016877	molecular_function	ligase activity, forming carbon-sulfur bonds
F	0019290	biological_process	siderophore biosynthetic process
F	0047527	molecular_function	2,3-dihydroxybenzoate-serine ligase activity
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005829	cellular_component	cytosol
G	0008668	molecular_function	2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
G	0009239	biological_process	enterobactin biosynthetic process
G	0016020	cellular_component	membrane
G	0016746	molecular_function	acyltransferase activity
G	0016874	molecular_function	ligase activity
G	0016877	molecular_function	ligase activity, forming carbon-sulfur bonds
G	0019290	biological_process	siderophore biosynthetic process
G	0047527	molecular_function	2,3-dihydroxybenzoate-serine ligase activity
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005829	cellular_component	cytosol
H	0008668	molecular_function	2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
H	0009239	biological_process	enterobactin biosynthetic process
H	0016020	cellular_component	membrane
H	0016746	molecular_function	acyltransferase activity
H	0016874	molecular_function	ligase activity
H	0016877	molecular_function	ligase activity, forming carbon-sulfur bonds
H	0019290	biological_process	siderophore biosynthetic process
H	0047527	molecular_function	2,3-dihydroxybenzoate-serine ligase activity
I	0005515	molecular_function	protein binding
I	0005524	molecular_function	ATP binding
I	0005829	cellular_component	cytosol
I	0008668	molecular_function	2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
I	0009239	biological_process	enterobactin biosynthetic process
I	0016020	cellular_component	membrane
I	0016746	molecular_function	acyltransferase activity
I	0016874	molecular_function	ligase activity
I	0016877	molecular_function	ligase activity, forming carbon-sulfur bonds
I	0019290	biological_process	siderophore biosynthetic process
I	0047527	molecular_function	2,3-dihydroxybenzoate-serine ligase activity
J	0005515	molecular_function	protein binding
J	0005524	molecular_function	ATP binding
J	0005829	cellular_component	cytosol
J	0008668	molecular_function	2,3-dihydroxybenzoate--[aryl-carrier protein] ligase
J	0009239	biological_process	enterobactin biosynthetic process
J	0016020	cellular_component	membrane
J	0016746	molecular_function	acyltransferase activity
J	0016874	molecular_function	ligase activity
J	0016877	molecular_function	ligase activity, forming carbon-sulfur bonds
J	0019290	biological_process	siderophore biosynthetic process
J	0047527	molecular_function	2,3-dihydroxybenzoate-serine ligase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE SVS A 698

Chain	Residue
A	ASN235
A	ALA335
A	ASP415
B	PNS991
A	TYR236
A	GLY309
A	ALA310
A	ARG311
A	VAL331
A	PHE332
A	GLY333
A	MET334

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PNS A 991

Chain	Residue
A	SER575
A	VAL576
B	PRO231
B	HIS234
B	PRO259
B	VAL279
B	GLY438
B	GLY439
B	SVS698

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SVS B 698

Chain	Residue
A	PNS991
B	ASN235
B	TYR236
B	GLY309
B	ALA310
B	ARG311
B	VAL331
B	PHE332
B	GLY333
B	MET334
B	ALA335
B	ASP415
B	ASN436

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PNS B 991

Chain	Residue
A	PRO231
A	HIS234
A	VAL279
A	GLY438
A	GLY439
A	GLU440
A	SVS698
B	SER575
B	VAL576

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SVS C 698

Chain	Residue
C	ASN235
C	TYR236
C	GLY309
C	ALA310
C	ARG311
C	VAL331
C	PHE332
C	GLY333
C	MET334
C	ALA335
C	ASP415
C	ASN436
H	PNS991

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PNS C 991

Chain	Residue
C	SER575
C	VAL576
H	PRO231
H	HIS234
H	VAL279
H	GLY438
H	GLY439
H	GLU440
H	SVS698

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE SVS D 698

Chain	Residue
D	ASN235
D	SER240
D	GLY309
D	ALA310
D	ARG311
D	VAL331
D	PHE332
D	GLY333
D	MET334
D	ALA335
D	VAL339
D	ASP415
D	ARG430
D	LYS441
E	PNS991

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PNS D 991

Chain	Residue
D	SER575
E	ILE230
E	HIS234
E	VAL279
E	GLY438
E	GLY439
E	SVS698

site_id	AC9
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SVS E 698

Chain	Residue
E	ASN436
D	PNS991
E	ASN235
E	TYR236
E	GLY309
E	ALA310
E	ARG311
E	VAL331
E	PHE332
E	GLY333
E	MET334
E	ALA335
E	ASP415

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PNS E 991

Chain	Residue
D	PRO231
D	HIS234
D	PRO259
D	VAL279
D	GLY438
D	GLY439
D	SVS698
E	SER575
E	VAL576

site_id	BC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SVS F 698

Chain	Residue
F	ASN235
F	GLY309
F	ALA310
F	ARG311
F	VAL331
F	PHE332
F	GLY333
F	MET334
F	ALA335
F	ASP415
F	LYS432
F	ASN436
I	PNS991

site_id	BC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PNS F 991

Chain	Residue
F	SER575
F	VAL576
I	ILE230
I	PRO231
I	HIS234
I	VAL279
I	GLY438
I	GLY439
I	MET470
I	SVS698

site_id	BC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SVS G 698

Chain	Residue
G	ASN235
G	TYR236
G	GLY309
G	ALA310
G	ARG311
G	VAL331
G	PHE332
G	GLY333
G	MET334
G	ALA335
G	ASP415
G	ASN436
J	PNS991

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PNS G 991

Chain	Residue
G	SER575
J	ILE230
J	PRO231
J	HIS234
J	GLY438
J	SVS698

site_id	BC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE SVS H 698

Chain	Residue
C	PNS991
H	ASN235
H	TYR236
H	GLY308
H	GLY309
H	ALA310
H	VAL331
H	PHE332
H	GLY333
H	MET334
H	ALA335
H	ASP415
H	VAL427
H	ASN436

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PNS H 991

Chain	Residue
C	PRO231
C	HIS234
C	VAL279
C	GLY438
C	GLY439
C	SVS698
H	SER575
H	VAL576

site_id	BC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE SVS I 698

Chain	Residue
F	PNS991
I	ASN235
I	TYR236
I	GLY309
I	ALA310
I	ARG311
I	VAL331
I	PHE332
I	GLY333
I	MET334
I	ALA335
I	ASP415
I	ARG430
I	LYS441

site_id	BC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PNS I 991

Chain	Residue
F	PRO231
F	HIS234
F	VAL279
F	GLY438
F	GLY439
F	GLU440
F	SVS698
I	SER575
I	VAL576

site_id	CC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SVS J 698

Chain	Residue
G	PNS991
J	ASN235
J	TYR236
J	GLY309
J	ALA310
J	ARG311
J	VAL331
J	PHE332
J	GLY333
J	MET334
J	ALA335
J	ASP415
J	ASN436

site_id	CC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PNS J 991

Chain	Residue
G	PRO231
G	HIS234
G	VAL279
G	GLY438
G	GLY439
G	SVS698
J	SER575
J	VAL576

site_id	CC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD B 616

Chain	Residue
B	SER190
B	LYS198

site_id	CC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD D 616

Chain	Residue
D	SER190
D	LYS198

site_id	CC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD I 616

Chain	Residue
I	SER190
I	PRO197

site_id	CC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD J 616

Chain	Residue
J	LYS198

site_id	CC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD A 616

Chain	Residue
A	TRP585

site_id	CC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD E 617

Chain	Residue
E	TRP585

site_id	CC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD H 616

Chain	Residue
H	PRO542
H	TRP585

site_id	DC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD I 617

Chain	Residue
I	TRP585

site_id	DC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD A 617

Chain	Residue
A	ARG7
A	TRP8

site_id	DC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD B 617

Chain	Residue
B	TRP8

site_id	DC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD G 616

Chain	Residue
G	ARG7
G	TRP8

site_id	DC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD D 618

Chain	Residue
D	PRO542
D	TRP585

site_id	DC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD J 617

Chain	Residue
J	TRP585

site_id	DC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IOD B 619

Chain	Residue
B	GLU18
B	LYS19

site_id	DC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD B 620

Chain	Residue
B	PRO321

site_id	DC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD I 618

Chain	Residue
I	GLU349

site_id	EC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD A 619

Chain	Residue
A	LEU328

Functional Information from PROSITE/UniProt

site_id	PS00455
Number of Residues	12
Details	AMP_BINDING Putative AMP-binding domain signature. FQLSGGTTGtPK

Chain	Residue	Details
A	PHE187-LYS198

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269\|PubMed:22365602

Chain	Residue	Details
A	ASN235
E	ALA335
F	ASN235
F	ALA335
G	ASN235
G	ALA335
H	ASN235
H	ALA335
I	ASN235
I	ALA335
J	ASN235
A	ALA335
J	ALA335
B	ASN235
B	ALA335
C	ASN235
C	ALA335
D	ASN235
D	ALA335
E	ASN235

site_id	SWS_FT_FI2
Number of Residues	30
Details	BINDING: BINDING => ECO:0000269\|PubMed:23897471

Chain	Residue	Details
A	SER240
D	SER240
D	LYS432
D	LYS441
E	SER240
E	LYS432
E	LYS441
F	SER240
F	LYS432
F	LYS441
G	SER240
A	LYS432
G	LYS432
G	LYS441
H	SER240
H	LYS432
H	LYS441
I	SER240
I	LYS432
I	LYS441
J	SER240
J	LYS432
A	LYS441
J	LYS441
B	SER240
B	LYS432
B	LYS441
C	SER240
C	LYS432
C	LYS441

site_id	SWS_FT_FI3
Number of Residues	30
Details	BINDING: BINDING => ECO:0000269\|PubMed:22365602, ECO:0000269\|PubMed:23897471

Chain	Residue	Details
A	GLY309
D	GLY309
D	VAL331
D	ASP415
E	GLY309
E	VAL331
E	ASP415
F	GLY309
F	VAL331
F	ASP415
G	GLY309
A	VAL331
G	VAL331
G	ASP415
H	GLY309
H	VAL331
H	ASP415
I	GLY309
I	VAL331
I	ASP415
J	GLY309
J	VAL331
A	ASP415
J	ASP415
B	GLY309
B	VAL331
B	ASP415
C	GLY309
C	VAL331
C	ASP415

site_id	SWS_FT_FI4
Number of Residues	30
Details	BINDING: BINDING => ECO:0000269\|PubMed:16632253, ECO:0007744\|PDB:2FQ1

Chain	Residue	Details
A	ASP557
D	ASP557
D	GLY572
D	ASP574
E	ASP557
E	GLY572
E	ASP574
F	ASP557
F	GLY572
F	ASP574
G	ASP557
A	GLY572
G	GLY572
G	ASP574
H	ASP557
H	GLY572
H	ASP574
I	ASP557
I	GLY572
I	ASP574
J	ASP557
J	GLY572
A	ASP574
J	ASP574
B	ASP557
B	GLY572
B	ASP574
C	ASP557
C	GLY572
C	ASP574

site_id	SWS_FT_FI5
Number of Residues	10
Details	MOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000269\|PubMed:22365602, ECO:0007744\|PDB:3RG2

Chain	Residue	Details
A	SER575
J	SER575
B	SER575
C	SER575
D	SER575
E	SER575
F	SER575
G	SER575
H	SER575
I	SER575

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