1YEY

Crystal Structure of L-fuconate Dehydratase from Xanthomonas campestris pv. campestris str. ATCC 33913

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0016052	biological_process	carbohydrate catabolic process
A	0016829	molecular_function	lyase activity
A	0016836	molecular_function	hydro-lyase activity
A	0046872	molecular_function	metal ion binding
A	0050023	molecular_function	L-fuconate dehydratase activity
B	0000287	molecular_function	magnesium ion binding
B	0016052	biological_process	carbohydrate catabolic process
B	0016829	molecular_function	lyase activity
B	0016836	molecular_function	hydro-lyase activity
B	0046872	molecular_function	metal ion binding
B	0050023	molecular_function	L-fuconate dehydratase activity
C	0000287	molecular_function	magnesium ion binding
C	0016052	biological_process	carbohydrate catabolic process
C	0016829	molecular_function	lyase activity
C	0016836	molecular_function	hydro-lyase activity
C	0046872	molecular_function	metal ion binding
C	0050023	molecular_function	L-fuconate dehydratase activity
D	0000287	molecular_function	magnesium ion binding
D	0016052	biological_process	carbohydrate catabolic process
D	0016829	molecular_function	lyase activity
D	0016836	molecular_function	hydro-lyase activity
D	0046872	molecular_function	metal ion binding
D	0050023	molecular_function	L-fuconate dehydratase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 6001

Chain	Residue
A	ASP248
A	ASN250
A	GLU274
A	GLU301
A	HOH5231
A	HOH5232

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 6002

Chain	Residue
B	GLU301
B	HOH5233
B	HOH5234
B	LYS220
B	ASP248
B	GLU274

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 6003

Chain	Residue
C	LYS220
C	ASP248
C	GLU274
C	GLU301
C	HOH5235
C	HOH5236

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG D 6004

Chain	Residue
D	LYS220
D	ASP248
D	ASN250
D	GLU274
D	GLU301
D	HOH5237
D	HOH5238

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:17144652

Chain	Residue	Details
A	LYS220
B	LYS220
C	LYS220
D	LYS220

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000255

Chain	Residue	Details
A	HIS351
B	HIS351
C	HIS351
D	HIS351

---

site_id	SWS_FT_FI3
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269|PubMed:17144652

Chain	Residue	Details
B	GLU274
B	GLU301
B	HIS351
B	GLU382
C	GLY22
C	TYR32
C	LYS218
C	ASN250
C	GLU274
C	GLU301
C	HIS351
C	GLU382
D	GLY22
D	TYR32
D	LYS218
D	ASN250
D	GLU274
D	GLU301
D	HIS351
D	GLU382
A	GLY22
A	TYR32
A	LYS218
A	ASN250
A	GLU274
A	GLU301
A	HIS351
A	GLU382
B	GLY22
B	TYR32
B	LYS218
B	ASN250

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:17144652, ECO:0000269|Ref.2

Chain	Residue	Details
A	ASP248
B	ASP248
C	ASP248
D	ASP248

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 961

Chain	Residue	Details
A	LYS220	proton acceptor, proton donor
A	ASP248	modifies pKa
A	GLU274	metal ligand
A	GLU301	metal ligand
A	ASP324	metal ligand
A	HIS351	proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	6
Details	M-CSA 961

Chain	Residue	Details
B	LYS220	proton acceptor, proton donor
B	ASP248	modifies pKa
B	GLU274	metal ligand
B	GLU301	metal ligand
B	ASP324	metal ligand
B	HIS351	proton acceptor, proton donor

---

site_id	MCSA3
Number of Residues	6
Details	M-CSA 961

Chain	Residue	Details
C	LYS220	proton acceptor, proton donor
C	ASP248	modifies pKa
C	GLU274	metal ligand
C	GLU301	metal ligand
C	ASP324	metal ligand
C	HIS351	proton acceptor, proton donor

---

site_id	MCSA4
Number of Residues	6
Details	M-CSA 961

Chain	Residue	Details
D	LYS220	proton acceptor, proton donor
D	ASP248	modifies pKa
D	GLU274	metal ligand
D	GLU301	metal ligand
D	ASP324	metal ligand
D	HIS351	proton acceptor, proton donor

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