Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3UXK

P. putida mandelate racemase co-crystallized with the intermediate analogue benzohydroxamate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0009063	biological_process	amino acid catabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016836	molecular_function	hydro-lyase activity
A	0016853	molecular_function	isomerase activity
A	0018838	molecular_function	mandelate racemase activity
A	0018924	biological_process	mandelate metabolic process
A	0019596	biological_process	mandelate catabolic process
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0009063	biological_process	amino acid catabolic process
B	0016052	biological_process	carbohydrate catabolic process
B	0016836	molecular_function	hydro-lyase activity
B	0016853	molecular_function	isomerase activity
B	0018838	molecular_function	mandelate racemase activity
B	0018924	biological_process	mandelate metabolic process
B	0019596	biological_process	mandelate catabolic process
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0009063	biological_process	amino acid catabolic process
C	0016052	biological_process	carbohydrate catabolic process
C	0016836	molecular_function	hydro-lyase activity
C	0016853	molecular_function	isomerase activity
C	0018838	molecular_function	mandelate racemase activity
C	0018924	biological_process	mandelate metabolic process
C	0019596	biological_process	mandelate catabolic process
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0009063	biological_process	amino acid catabolic process
D	0016052	biological_process	carbohydrate catabolic process
D	0016836	molecular_function	hydro-lyase activity
D	0016853	molecular_function	isomerase activity
D	0018838	molecular_function	mandelate racemase activity
D	0018924	biological_process	mandelate metabolic process
D	0019596	biological_process	mandelate catabolic process
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 360

Chain	Residue
A	ASP195
A	GLU221
A	GLU247
A	BHO361
A	HOH722

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BHO A 361

Chain	Residue
A	GLU221
A	GLU247
A	HIS297
A	GLU317
A	MG360
A	HOH722
A	LYS164
A	LYS166
A	ASP195
A	ASN197

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 360

Chain	Residue
B	ASP195
B	GLU221
B	GLU247
B	BHO361
B	HOH723

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BHO B 361

Chain	Residue
B	LYS164
B	LYS166
B	ASP195
B	ASN197
B	GLU221
B	GLU247
B	HIS297
B	GLU317
B	MG360
B	HOH723

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 360

Chain	Residue
C	ASP195
C	GLU221
C	GLU247
C	BHO361
C	HOH721

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BHO C 361

Chain	Residue
C	LYS164
C	LYS166
C	ASP195
C	ASN197
C	GLU221
C	GLU247
C	HIS297
C	GLU317
C	MG360

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 360

Chain	Residue
D	ASP195
D	GLU221
D	GLU247
D	BHO361
D	HOH724

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BHO D 361

Chain	Residue
D	LYS164
D	LYS166
D	ASP195
D	ASN197
D	GLU221
D	GLU247
D	HIS297
D	GLU317
D	MG360
D	HOH724

Functional Information from PROSITE/UniProt

site_id	PS00908
Number of Residues	26
Details	MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AaAGIDmAAwDAlGKvhetPLvkLLG

Chain	Residue	Details
A	ALA103-GLY128

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

Chain	Residue	Details
A	ILE192-PRO223

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor; specific for S-mandelate"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor; specific for R-mandelate"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7893689","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7893690","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1892834","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	9
Details	M-CSA 187

Chain	Residue	Details
A	LYS164	electrostatic stabiliser, hydrogen bond donor
A	LYS166	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASP195	metal ligand
A	ASN197	electrostatic stabiliser
A	GLU221	metal ligand
A	GLU247	metal ligand
A	ASP270	electrostatic stabiliser, hydrogen bond acceptor, increase basicity
A	HIS297	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLU317	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	9
Details	M-CSA 187

Chain	Residue	Details
B	LYS164	electrostatic stabiliser, hydrogen bond donor
B	LYS166	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ASP195	metal ligand
B	ASN197	electrostatic stabiliser
B	GLU221	metal ligand
B	GLU247	metal ligand
B	ASP270	electrostatic stabiliser, hydrogen bond acceptor, increase basicity
B	HIS297	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	GLU317	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA3
Number of Residues	9
Details	M-CSA 187

Chain	Residue	Details
C	LYS164	electrostatic stabiliser, hydrogen bond donor
C	LYS166	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ASP195	metal ligand
C	ASN197	electrostatic stabiliser
C	GLU221	metal ligand
C	GLU247	metal ligand
C	ASP270	electrostatic stabiliser, hydrogen bond acceptor, increase basicity
C	HIS297	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	GLU317	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA4
Number of Residues	9
Details	M-CSA 187

Chain	Residue	Details
D	LYS164	electrostatic stabiliser, hydrogen bond donor
D	LYS166	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	ASP195	metal ligand
D	ASN197	electrostatic stabiliser
D	GLU221	metal ligand
D	GLU247	metal ligand
D	ASP270	electrostatic stabiliser, hydrogen bond acceptor, increase basicity
D	HIS297	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	GLU317	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

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