Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2PP1

Crystal structure of L-talarate/galactarate dehydratase from Salmonella typhimurium LT2 liganded with Mg and L-lyxarohydroxamate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0008867	molecular_function	galactarate dehydratase activity
A	0009063	biological_process	amino acid catabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016829	molecular_function	lyase activity
A	0016836	molecular_function	hydro-lyase activity
A	0046392	biological_process	galactarate catabolic process
A	0046872	molecular_function	metal ion binding
A	1903663	biological_process	L-altrarate catabolic process
A	1990594	molecular_function	L-altrarate dehydratase activity
B	0000287	molecular_function	magnesium ion binding
B	0008867	molecular_function	galactarate dehydratase activity
B	0009063	biological_process	amino acid catabolic process
B	0016052	biological_process	carbohydrate catabolic process
B	0016829	molecular_function	lyase activity
B	0016836	molecular_function	hydro-lyase activity
B	0046392	biological_process	galactarate catabolic process
B	0046872	molecular_function	metal ion binding
B	1903663	biological_process	L-altrarate catabolic process
B	1990594	molecular_function	L-altrarate dehydratase activity
C	0000287	molecular_function	magnesium ion binding
C	0008867	molecular_function	galactarate dehydratase activity
C	0009063	biological_process	amino acid catabolic process
C	0016052	biological_process	carbohydrate catabolic process
C	0016829	molecular_function	lyase activity
C	0016836	molecular_function	hydro-lyase activity
C	0046392	biological_process	galactarate catabolic process
C	0046872	molecular_function	metal ion binding
C	1903663	biological_process	L-altrarate catabolic process
C	1990594	molecular_function	L-altrarate dehydratase activity
D	0000287	molecular_function	magnesium ion binding
D	0008867	molecular_function	galactarate dehydratase activity
D	0009063	biological_process	amino acid catabolic process
D	0016052	biological_process	carbohydrate catabolic process
D	0016829	molecular_function	lyase activity
D	0016836	molecular_function	hydro-lyase activity
D	0046392	biological_process	galactarate catabolic process
D	0046872	molecular_function	metal ion binding
D	1903663	biological_process	L-altrarate catabolic process
D	1990594	molecular_function	L-altrarate dehydratase activity
E	0000287	molecular_function	magnesium ion binding
E	0008867	molecular_function	galactarate dehydratase activity
E	0009063	biological_process	amino acid catabolic process
E	0016052	biological_process	carbohydrate catabolic process
E	0016829	molecular_function	lyase activity
E	0016836	molecular_function	hydro-lyase activity
E	0046392	biological_process	galactarate catabolic process
E	0046872	molecular_function	metal ion binding
E	1903663	biological_process	L-altrarate catabolic process
E	1990594	molecular_function	L-altrarate dehydratase activity
F	0000287	molecular_function	magnesium ion binding
F	0008867	molecular_function	galactarate dehydratase activity
F	0009063	biological_process	amino acid catabolic process
F	0016052	biological_process	carbohydrate catabolic process
F	0016829	molecular_function	lyase activity
F	0016836	molecular_function	hydro-lyase activity
F	0046392	biological_process	galactarate catabolic process
F	0046872	molecular_function	metal ion binding
F	1903663	biological_process	L-altrarate catabolic process
F	1990594	molecular_function	L-altrarate dehydratase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 399

Chain	Residue
A	LYS195
A	ASP226
A	GLU252
A	GLU278
A	LLH801
A	HOH944

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 444

Chain	Residue
B	GLU278
B	LLH802
B	HOH939
B	LYS195
B	ASP226
B	GLU252

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE LLH A 801

Chain	Residue
A	ASP46
A	LYS48
A	LYS82
A	ARG83
A	PHE171
A	LYS195
A	LYS197
A	ASP226
A	ASN228
A	GLU278
A	HIS328
A	GLU348
A	TRP352
A	MG399
A	HOH811
A	HOH938
A	HOH939

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE LLH B 802

Chain	Residue
B	ASP46
B	LYS48
B	LYS82
B	ARG83
B	PHE171
B	LYS195
B	LYS197
B	ASP226
B	ASN228
B	GLU278
B	HIS328
B	GLU348
B	TRP352
B	MG444
B	HOH814
B	HOH931
B	HOH937

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE LLH C 803

Chain	Residue
C	ASP46
C	LYS48
C	LYS82
C	ARG83
C	PHE171
C	LYS195
C	LYS197
C	ASP226
C	ASN228
C	GLU278
C	HIS328
C	GLU348
C	TRP352
C	HOH818
C	HOH855
C	HOH868
C	HOH874

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE LLH D 804

Chain	Residue
D	ASP46
D	LYS48
D	LYS82
D	ARG83
D	PHE171
D	LYS195
D	LYS197
D	ASP226
D	ASN228
D	GLU278
D	HIS328
D	GLU348
D	TRP352
D	HOH827
D	HOH834
D	HOH862
D	HOH869

site_id	AC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE LLH E 805

Chain	Residue
E	ASP46
E	LYS48
E	LYS82
E	ARG83
E	PHE171
E	LYS195
E	LYS197
E	ASP226
E	ASN228
E	GLU252
E	GLU278
E	HIS328
E	GLU348
E	TRP352
E	HOH819
E	HOH880
E	HOH891
E	HOH895

site_id	AC8
Number of Residues	18
Details	BINDING SITE FOR RESIDUE LLH F 806

Chain	Residue
F	LYS48
F	LYS82
F	ARG83
F	PHE171
F	LYS195
F	LYS197
F	ASP226
F	ASN228
F	GLU252
F	GLU278
F	HIS328
F	GLU348
F	TRP352
F	HOH830
F	HOH844
F	HOH884
F	HOH891
F	ASP46

Functional Information from PROSITE/UniProt

site_id	PS00909
Number of Residues	32
Details	MR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. LmvDaNqqwdretAirmgrkMeqfnliwIEEP

Chain	Residue	Details
A	LEU223-PRO254

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:17649980

Chain	Residue	Details
A	LYS197
B	LYS197
C	LYS197
D	LYS197
E	LYS197
F	LYS197

site_id	SWS_FT_FI2
Number of Residues	6
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269\|PubMed:17649980

Chain	Residue	Details
A	HIS328
B	HIS328
C	HIS328
D	HIS328
E	HIS328
F	HIS328

site_id	SWS_FT_FI3
Number of Residues	48
Details	BINDING: BINDING => ECO:0000269\|PubMed:17649980

Chain	Residue	Details
A	ASP46
B	LYS82
B	LYS195
B	ASP226
B	ASN228
B	GLU252
B	GLU278
B	GLU348
C	ASP46
C	LYS82
C	LYS195
A	LYS82
C	ASP226
C	ASN228
C	GLU252
C	GLU278
C	GLU348
D	ASP46
D	LYS82
D	LYS195
D	ASP226
D	ASN228
A	LYS195
D	GLU252
D	GLU278
D	GLU348
E	ASP46
E	LYS82
E	LYS195
E	ASP226
E	ASN228
E	GLU252
E	GLU278
A	ASP226
E	GLU348
F	ASP46
F	LYS82
F	LYS195
F	ASP226
F	ASN228
F	GLU252
F	GLU278
F	GLU348
A	ASN228
A	GLU252
A	GLU278
A	GLU348
B	ASP46

site_id	SWS_FT_FI4
Number of Residues	6
Details	SITE: Increases basicity of active site His

Chain	Residue	Details
A	ASP301
B	ASP301
C	ASP301
D	ASP301
E	ASP301
F	ASP301

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1mdr

Chain	Residue	Details
A	HIS328
A	GLU348
A	LYS197
A	ASP301

site_id	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1mdr

Chain	Residue	Details
D	LYS195
D	PRO355
D	LYS197

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1mdr

Chain	Residue	Details
E	LYS195
E	PRO355
E	LYS197

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1mdr

Chain	Residue	Details
F	LYS195
F	PRO355
F	LYS197

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

Chain	Residue	Details
B	HIS328
B	GLU348
B	LYS197
B	ASP301

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1mdr

Chain	Residue	Details
C	HIS328
C	GLU348
C	LYS197
C	ASP301

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

Chain	Residue	Details
D	HIS328
D	GLU348
D	LYS197
D	ASP301

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1mdr

Chain	Residue	Details
E	HIS328
E	GLU348
E	LYS197
E	ASP301

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1mdr

Chain	Residue	Details
F	HIS328
F	GLU348
F	LYS197
F	ASP301

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

Chain	Residue	Details
A	LYS195
A	PRO355
A	LYS197

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

Chain	Residue	Details
B	LYS195
B	PRO355
B	LYS197

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1mdr

Chain	Residue	Details
C	LYS195
C	PRO355
C	LYS197

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