2DW6

Crystal structure of the mutant K184A of D-Tartrate Dehydratase from Bradyrhizobium japonicum complexed with Mg++ and D-tartrate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding
A	0047808	molecular_function	D(-)-tartrate dehydratase activity
A	0051260	biological_process	protein homooligomerization
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0016829	molecular_function	lyase activity
B	0046872	molecular_function	metal ion binding
B	0047808	molecular_function	D(-)-tartrate dehydratase activity
B	0051260	biological_process	protein homooligomerization
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0016829	molecular_function	lyase activity
C	0046872	molecular_function	metal ion binding
C	0047808	molecular_function	D(-)-tartrate dehydratase activity
C	0051260	biological_process	protein homooligomerization
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0016829	molecular_function	lyase activity
D	0046872	molecular_function	metal ion binding
D	0047808	molecular_function	D(-)-tartrate dehydratase activity
D	0051260	biological_process	protein homooligomerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 2001

Chain	Residue
A	ASP213
A	GLU239
A	GLU265
A	TAR1001
A	HOH2002

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 2002

Chain	Residue
B	HOH2003
B	ASP213
B	GLU239
B	GLU265
B	TAR1002

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 2003

Chain	Residue
C	ASP213
C	GLU239
C	GLU265
C	TAR1003
C	HOH2004

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 2004

Chain	Residue
D	LYS182
D	ASP213
D	GLU239
D	GLU265
D	TLA1004
D	HOH2005

---

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TLA D 1004

Chain	Residue
C	LYS102
D	ASN21
D	PHE26
D	TYR156
D	LYS182
D	ASP213
D	ASN215
D	GLU239
D	GLU265
D	HIS322
D	GLU341
D	TYR343
D	MG2004
D	HOH2005
D	HOH2112

---

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TAR A 1001

Chain	Residue
A	ASN21
A	PHE26
A	ASN55
A	TYR156
A	LYS182
A	ASP213
A	ASN215
A	GLU239
A	GLU265
A	HIS322
A	GLU341
A	TYR343
A	MG2001
A	HOH2002
B	LYS102

---

site_id	AC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE TAR B 1002

Chain	Residue
A	LYS102
B	ASN21
B	PHE26
B	ASN55
B	TYR156
B	LYS182
B	ASP213
B	ASN215
B	GLU239
B	GLU265
B	HIS322
B	GLU341
B	TYR343
B	MG2002
B	HOH2003
B	HOH2073

---

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE TAR C 1003

Chain	Residue
C	ASN21
C	PHE26
C	ASN55
C	TYR156
C	LYS182
C	ASP213
C	ASN215
C	GLU239
C	GLU265
C	HIS322
C	GLU341
C	TYR343
C	MG2003
C	HOH2004
C	HOH2040
D	LYS102

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: acceptor => ECO:0000269|PubMed:17144653

Chain	Residue	Details
A	ALA184
B	ALA184
C	ALA184
D	ALA184

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:17144653

Chain	Residue	Details
A	HIS322
B	HIS322
C	HIS322
D	HIS322

---

site_id	SWS_FT_FI3
Number of Residues	36
Details	BINDING:

Chain	Residue	Details
A	ASN21
B	ASN21
B	ASN55
B	LYS102
B	TYR156
B	LYS182
B	GLU239
B	GLU265
B	HIS322
B	GLU341
C	ASN21
A	ASN55
C	ASN55
C	LYS102
C	TYR156
C	LYS182
C	GLU239
C	GLU265
C	HIS322
C	GLU341
D	ASN21
D	ASN55
A	LYS102
D	LYS102
D	TYR156
D	LYS182
D	GLU239
D	GLU265
D	HIS322
D	GLU341
A	TYR156
A	LYS182
A	GLU239
A	GLU265
A	HIS322
A	GLU341

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:17144653

Chain	Residue	Details
A	ASP213
B	ASP213
C	ASP213
D	ASP213

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	SITE: Transition state stabilizer

Chain	Residue	Details
A	ASN55
D	ASN55
D	LYS182
D	GLU341
A	LYS182
A	GLU341
B	ASN55
B	LYS182
B	GLU341
C	ASN55
C	LYS182
C	GLU341

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	SITE: Increases basicity of active site His

Chain	Residue	Details
A	ASP292
B	ASP292
C	ASP292
D	ASP292

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	9
Details	M-CSA 463

Chain	Residue	Details
A	ASN55	electrostatic stabiliser
A	LYS182	electrostatic stabiliser
A	ALA184	proton acceptor, proton donor
A	ASP213	metal ligand
A	GLU239	metal ligand
A	GLU265	metal ligand
A	ASP292	electrostatic stabiliser, increase basicity, modifies pKa
A	HIS322	proton acceptor, proton donor
A	GLU341	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	9
Details	M-CSA 463

Chain	Residue	Details
B	ASN55	electrostatic stabiliser
B	LYS182	electrostatic stabiliser
B	ALA184	proton acceptor, proton donor
B	ASP213	metal ligand
B	GLU239	metal ligand
B	GLU265	metal ligand
B	ASP292	electrostatic stabiliser, increase basicity, modifies pKa
B	HIS322	proton acceptor, proton donor
B	GLU341	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	9
Details	M-CSA 463

Chain	Residue	Details
C	ASN55	electrostatic stabiliser
C	LYS182	electrostatic stabiliser
C	ALA184	proton acceptor, proton donor
C	ASP213	metal ligand
C	GLU239	metal ligand
C	GLU265	metal ligand
C	ASP292	electrostatic stabiliser, increase basicity, modifies pKa
C	HIS322	proton acceptor, proton donor
C	GLU341	electrostatic stabiliser

---

site_id	MCSA4
Number of Residues	9
Details	M-CSA 463

Chain	Residue	Details
D	ASN55	electrostatic stabiliser
D	LYS182	electrostatic stabiliser
D	ALA184	proton acceptor, proton donor
D	ASP213	metal ligand
D	GLU239	metal ligand
D	GLU265	metal ligand
D	ASP292	electrostatic stabiliser, increase basicity, modifies pKa
D	HIS322	proton acceptor, proton donor
D	GLU341	electrostatic stabiliser

---