3PWG

Crystal structure of the mutant S29G.P34A of D-Glucarate dehydratase from Escherichia coli complexed with product 5-keto-4-deoxy-D-Glucarate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0008872	molecular_function	glucarate dehydratase activity
A	0016829	molecular_function	lyase activity
A	0019394	biological_process	glucarate catabolic process
A	0042838	biological_process	D-glucarate catabolic process
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0008872	molecular_function	glucarate dehydratase activity
B	0016829	molecular_function	lyase activity
B	0019394	biological_process	glucarate catabolic process
B	0042838	biological_process	D-glucarate catabolic process
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0008872	molecular_function	glucarate dehydratase activity
C	0016829	molecular_function	lyase activity
C	0019394	biological_process	glucarate catabolic process
C	0042838	biological_process	D-glucarate catabolic process
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0008872	molecular_function	glucarate dehydratase activity
D	0016829	molecular_function	lyase activity
D	0019394	biological_process	glucarate catabolic process
D	0042838	biological_process	D-glucarate 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 447

Chain	Residue
A	ASP235
A	GLU260
A	ASN289
A	GLR448
A	HOH502

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 447

Chain	Residue
B	HOH514
B	ASP235
B	GLU260
B	ASN289
B	GLR448

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 447

Chain	Residue
C	ASP235
C	ASN237
C	GLU260
C	ASN289
C	GLR448
C	HOH474

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 447

Chain	Residue
D	ASP235
D	ASN237
D	GLU260
D	ASN289
D	GLR448
D	HOH463

---

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE GLR A 448

Chain	Residue
A	ASN27
A	HIS32
A	THR103
A	TYR150
A	LYS205
A	LYS207
A	ASP235
A	ASN237
A	GLU260
A	ASN289
A	HIS339
A	SER340
A	ASN341
A	HIS368
A	ARG422
A	MG447
A	HOH488

---

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE GLR B 448

Chain	Residue
B	ASN27
B	HIS32
B	THR103
B	PHE104
B	TYR150
B	LYS205
B	LYS207
B	ASP235
B	ASN237
B	GLU260
B	ASN289
B	HIS339
B	SER340
B	ASN341
B	HIS368
B	ARG422
B	MG447
B	HOH451

---

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE GLR C 448

Chain	Residue
C	ASN27
C	HIS32
C	TYR150
C	PHE152
C	LYS205
C	LYS207
C	ASP235
C	ASN237
C	GLU260
C	ASN289
C	SER340
C	ASN341
C	HIS368
C	ARG422
C	MG447

---

site_id	AC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE GLR D 448

Chain	Residue
D	ASN27
D	HIS32
D	TYR150
D	PHE152
D	LYS205
D	LYS207
D	ASP235
D	ASN237
D	GLU260
D	ASN289
D	SER340
D	HIS368
D	ARG422
D	MG447

---

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 449

Chain	Residue
A	GLY299
A	SER303
A	HOH481
A	HOH485
B	ARG280
C	LEU302
C	PHE332

---

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 449

Chain	Residue
D	PHE332
A	ARG280
B	GLY299
B	SER303
B	HOH483
D	LEU302
D	GLN305

---

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 449

Chain	Residue
B	LEU302
B	PHE332
B	HOH483
C	ARG280
D	GLY299
D	SER303
D	HOH456

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:11513584

Chain	Residue	Details
A	LYS207
A	HIS339
B	LYS207
B	HIS339
C	LYS207
C	HIS339
D	LYS207
D	HIS339

---

site_id	SWS_FT_FI2
Number of Residues	32
Details	BINDING:

Chain	Residue	Details
A	HIS32
B	THR103
B	TYR150
B	LYS205
B	ASN289
B	HIS339
B	HIS368
B	ARG422
C	HIS32
C	THR103
C	TYR150
A	THR103
C	LYS205
C	ASN289
C	HIS339
C	HIS368
C	ARG422
D	HIS32
D	THR103
D	TYR150
D	LYS205
D	ASN289
A	TYR150
D	HIS339
D	HIS368
D	ARG422
A	LYS205
A	ASN289
A	HIS339
A	HIS368
A	ARG422
B	HIS32

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:11513584

Chain	Residue	Details
A	ASP235
A	GLU266
B	ASP235
B	GLU266
C	ASP235
C	GLU266
D	ASP235
D	GLU266

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	9
Details	M-CSA 451

Chain	Residue	Details
A	LYS205	electrostatic stabiliser
A	LYS207	electrostatic stabiliser
A	ASP235	metal ligand
A	ASN237	activator, electrostatic stabiliser
A	GLU260	metal ligand
A	ASN289	metal ligand
A	ASP313	electrostatic stabiliser, modifies pKa
A	HIS339	proton acceptor, proton donor
A	ASN341	activator

---

site_id	MCSA2
Number of Residues	9
Details	M-CSA 451

Chain	Residue	Details
B	LYS205	electrostatic stabiliser
B	LYS207	electrostatic stabiliser
B	ASP235	metal ligand
B	ASN237	activator, electrostatic stabiliser
B	GLU260	metal ligand
B	ASN289	metal ligand
B	ASP313	electrostatic stabiliser, modifies pKa
B	HIS339	proton acceptor, proton donor
B	ASN341	activator

---

site_id	MCSA3
Number of Residues	9
Details	M-CSA 451

Chain	Residue	Details
C	LYS205	electrostatic stabiliser
C	LYS207	electrostatic stabiliser
C	ASP235	metal ligand
C	ASN237	activator, electrostatic stabiliser
C	GLU260	metal ligand
C	ASN289	metal ligand
C	ASP313	electrostatic stabiliser, modifies pKa
C	HIS339	proton acceptor, proton donor
C	ASN341	activator

---

site_id	MCSA4
Number of Residues	9
Details	M-CSA 451

Chain	Residue	Details
D	LYS205	electrostatic stabiliser
D	LYS207	electrostatic stabiliser
D	ASP235	metal ligand
D	ASN237	activator, electrostatic stabiliser
D	GLU260	metal ligand
D	ASN289	metal ligand
D	ASP313	electrostatic stabiliser, modifies pKa
D	HIS339	proton acceptor, proton donor
D	ASN341	activator

---