Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2IHU

Carboxyethylarginine synthase from Streptomyces clavuligerus: putative reaction intermediate complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0003984	molecular_function	acetolactate synthase activity
A	0005948	cellular_component	acetolactate synthase complex
A	0009097	biological_process	isoleucine biosynthetic process
A	0009099	biological_process	L-valine biosynthetic process
A	0016740	molecular_function	transferase activity
A	0030976	molecular_function	thiamine pyrophosphate binding
A	0033848	molecular_function	N2-(2-carboxyethyl)arginine synthase activity
A	0046872	molecular_function	metal ion binding
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0003984	molecular_function	acetolactate synthase activity
B	0005948	cellular_component	acetolactate synthase complex
B	0009097	biological_process	isoleucine biosynthetic process
B	0009099	biological_process	L-valine biosynthetic process
B	0016740	molecular_function	transferase activity
B	0030976	molecular_function	thiamine pyrophosphate binding
B	0033848	molecular_function	N2-(2-carboxyethyl)arginine synthase activity
B	0046872	molecular_function	metal ion binding
B	0050660	molecular_function	flavin adenine dinucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0003984	molecular_function	acetolactate synthase activity
C	0005948	cellular_component	acetolactate synthase complex
C	0009097	biological_process	isoleucine biosynthetic process
C	0009099	biological_process	L-valine biosynthetic process
C	0016740	molecular_function	transferase activity
C	0030976	molecular_function	thiamine pyrophosphate binding
C	0033848	molecular_function	N2-(2-carboxyethyl)arginine synthase activity
C	0046872	molecular_function	metal ion binding
C	0050660	molecular_function	flavin adenine dinucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0003984	molecular_function	acetolactate synthase activity
D	0005948	cellular_component	acetolactate synthase complex
D	0009097	biological_process	isoleucine biosynthetic process
D	0009099	biological_process	L-valine biosynthetic process
D	0016740	molecular_function	transferase activity
D	0030976	molecular_function	thiamine pyrophosphate binding
D	0033848	molecular_function	N2-(2-carboxyethyl)arginine synthase activity
D	0046872	molecular_function	metal ion binding
D	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 601

Chain	Residue
A	ASP463
A	ASN490
A	THR492
A	TP9600
A	HOH1755

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K A 602

Chain	Residue
A	GLU396
A	GLU397
A	ALA399

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 601

Chain	Residue
B	ASN490
B	THR492
B	TP9600
B	HOH868
B	ASP463

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K B 602

Chain	Residue
B	GLU396
B	GLU397
B	ALA399
B	HOH898

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 601

Chain	Residue
C	ASP463
C	ASN490
C	THR492
C	TP8600
C	HOH1733

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K C 602

Chain	Residue
C	GLU396
C	GLU397
C	ALA399

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 601

Chain	Residue
D	ASP463
D	ASN490
D	THR492
D	TP9600
D	HOH827

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K D 602

Chain	Residue
D	GLU396
D	GLU397
D	ALA399

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE K A 1501

Chain	Residue
A	HIS56
A	SER468
A	HOH1536
A	HOH1751
B	HIS56
B	SER468
B	HOH652
B	HOH929

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE K C 1502

Chain	Residue
C	HIS56
C	SER468
C	HOH1537
C	HOH1723
D	HIS56
D	SER468
D	HOH675
D	HOH789

site_id	BC2
Number of Residues	27
Details	BINDING SITE FOR RESIDUE TP9 A 600

Chain	Residue
A	ILE410
A	GLY411
A	PHE412
A	PHE413
A	SER436
A	SER437
A	PHE438
A	GLY462
A	ASP463
A	GLY464
A	GLY465
A	ASN490
A	THR492
A	ASN493
A	GLY494
A	LEU495
A	TYR561
A	MG601
A	TAR603
A	HOH1750
A	HOH1755
B	VAL34
B	GLY35
B	GLU57
B	THR80
B	PRO83
B	ASN87

site_id	BC3
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TP9 B 600

Chain	Residue
B	HOH864
B	HOH868
A	GLY35
A	GLU57
A	THR80
A	PRO83
A	ASN87
B	ILE410
B	GLY411
B	PHE412
B	PHE413
B	SER436
B	SER437
B	PHE438
B	GLY462
B	ASP463
B	GLY464
B	GLY465
B	ASN490
B	THR492
B	ASN493
B	GLY494
B	LEU495
B	TYR561
B	MG601

site_id	BC4
Number of Residues	32
Details	BINDING SITE FOR RESIDUE TP8 C 600

Chain	Residue
C	ILE410
C	GLY411
C	PHE412
C	PHE413
C	SER436
C	SER437
C	PHE438
C	GLY462
C	ASP463
C	GLY464
C	GLY465
C	ASN490
C	THR492
C	ASN493
C	GLY494
C	LEU495
C	ILE496
C	TYR499
C	TYR561
C	TP8600
C	MG601
C	HOH1676
C	HOH1687
C	HOH1733
C	HOH1794
D	GLY35
D	GLU57
D	THR80
D	PRO83
D	ASN87
D	HIS120
D	GLN121

site_id	BC5
Number of Residues	32
Details	BINDING SITE FOR RESIDUE TP8 C 600

Chain	Residue
C	ILE410
C	GLY411
C	PHE412
C	PHE413
C	SER436
C	SER437
C	PHE438
C	GLY462
C	ASP463
C	GLY464
C	GLY465
C	ASN490
C	THR492
C	ASN493
C	GLY494
C	LEU495
C	ILE496
C	TYR499
C	TYR561
C	TP8600
C	MG601
C	HOH1676
C	HOH1687
C	HOH1733
C	HOH1794
D	GLY35
D	GLU57
D	THR80
D	PRO83
D	ASN87
D	HIS120
D	GLN121

site_id	BC6
Number of Residues	27
Details	BINDING SITE FOR RESIDUE TP9 D 600

Chain	Residue
C	VAL34
C	GLY35
C	GLU57
C	THR80
C	PRO83
C	ASN87
D	ILE410
D	GLY411
D	PHE412
D	PHE413
D	SER436
D	SER437
D	PHE438
D	GLY462
D	ASP463
D	GLY464
D	GLY465
D	ASN490
D	THR492
D	ASN493
D	GLY494
D	LEU495
D	TYR561
D	MG601
D	TAR603
D	HOH825
D	HOH827

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TAR A 603

Chain	Residue
A	TYR271
A	ILE410
A	ARG414
A	HIS415
A	LEU495
A	TP9600
A	HOH1581
A	HOH1614
A	HOH1615
B	HIS120
B	GLN121

site_id	BC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TAR D 603

Chain	Residue
C	HIS120
C	GLN121
D	TYR271
D	ILE410
D	ARG414
D	HIS415
D	SER436
D	LEU495
D	TP9600
D	HOH869

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 603

Chain	Residue
B	ARG367
B	GLU370
B	PHE371
B	ASP374

Functional Information from PROSITE/UniProt

site_id	PS00187
Number of Residues	20
Details	TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGaqmarPdqptFlIaGDGG

Chain	Residue	Details
A	ILE446-GLY465

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	13
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19477162","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	60
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14623876","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19477162","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 367

Chain	Residue	Details
A	GLU57	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	PHE438	steric role
A	ASP463	metal ligand
A	ASN490	metal ligand
A	THR492	metal ligand
A	TYR561	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA2
Number of Residues	6
Details	M-CSA 367

Chain	Residue	Details
B	GLU57	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	PHE438	steric role
B	ASP463	metal ligand
B	ASN490	metal ligand
B	THR492	metal ligand
B	TYR561	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA3
Number of Residues	6
Details	M-CSA 367

Chain	Residue	Details
C	GLU57	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	PHE438	steric role
C	ASP463	metal ligand
C	ASN490	metal ligand
C	THR492	metal ligand
C	TYR561	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA4
Number of Residues	6
Details	M-CSA 367

Chain	Residue	Details
D	GLU57	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	PHE438	steric role
D	ASP463	metal ligand
D	ASN490	metal ligand
D	THR492	metal ligand
D	TYR561	electrostatic stabiliser, hydrogen bond acceptor

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