3VNK

Crystal structures of D-Psicose 3-epimerase with D-fructose from Clostridium cellulolyticum H10

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016853	molecular_function	isomerase activity
A	0016857	molecular_function	racemase and epimerase activity, acting on carbohydrates and derivatives
A	0030145	molecular_function	manganese ion binding
A	0046872	molecular_function	metal ion binding
A	0050897	molecular_function	cobalt ion binding
B	0016853	molecular_function	isomerase activity
B	0016857	molecular_function	racemase and epimerase activity, acting on carbohydrates and derivatives
B	0030145	molecular_function	manganese ion binding
B	0046872	molecular_function	metal ion binding
B	0050897	molecular_function	cobalt ion binding
C	0016853	molecular_function	isomerase activity
C	0016857	molecular_function	racemase and epimerase activity, acting on carbohydrates and derivatives
C	0030145	molecular_function	manganese ion binding
C	0046872	molecular_function	metal ion binding
C	0050897	molecular_function	cobalt ion binding
D	0016853	molecular_function	isomerase activity
D	0016857	molecular_function	racemase and epimerase activity, acting on carbohydrates and derivatives
D	0030145	molecular_function	manganese ion binding
D	0046872	molecular_function	metal ion binding
D	0050897	molecular_function	cobalt ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE FUD A 301

Chain	Residue
A	TYR6
A	PHE246
A	MN302
A	HOH401
A	HOH591
A	TRP112
A	GLU150
A	GLU156
A	ASP183
A	HIS186
A	HIS209
A	ARG215
A	GLU244

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 302

Chain	Residue
A	GLU150
A	ASP183
A	HIS209
A	GLU244
A	FUD301

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE FUD B 1301

Chain	Residue
B	TYR6
B	TRP14
B	TRP112
B	GLU150
B	GLU156
B	ASP183
B	HIS186
B	HIS209
B	ARG215
B	GLU244
B	MN1302
B	HOH1450
B	HOH1491
B	HOH1591

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN B 1302

Chain	Residue
B	GLU150
B	ASP183
B	HIS209
B	GLU244
B	FUD1301

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN B 1303

Chain	Residue
B	ASP192
B	HOH1583
C	HOH450
D	HOH500

---

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE FUD C 301

Chain	Residue
C	TYR6
C	TRP14
C	TRP112
C	GLU150
C	GLU156
C	ASP183
C	HIS186
C	HIS209
C	ARG215
C	GLU244
C	MN302
C	HOH422
C	HOH424
C	HOH547

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 302

Chain	Residue
C	GLU150
C	ASP183
C	HIS209
C	GLU244
C	FUD301

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MN C 303

Chain	Residue
B	HOH1583
C	ARG220

---

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE FUD D 301

Chain	Residue
D	TYR6
D	TRP14
D	TRP112
D	GLU150
D	GLU156
D	ASP183
D	HIS186
D	HIS209
D	ARG215
D	GLU244
D	MN302
D	HOH405
D	HOH437
D	HOH453

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN D 302

Chain	Residue
D	GLU150
D	ASP183
D	HIS209
D	GLU244
D	FUD301

---

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN D 303

Chain	Residue
B	HOH1470
D	ASP192
D	HOH522

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q9WYP7

Chain	Residue	Details
A	GLU150
A	GLU244
B	GLU150
B	GLU244
C	GLU150
C	GLU244
D	GLU150
D	GLU244

---

site_id	SWS_FT_FI2
Number of Residues	28
Details	BINDING: BINDING => ECO:0000269|PubMed:22426981

Chain	Residue	Details
A	TYR6
B	GLU156
B	ASP183
B	HIS209
B	ARG215
B	GLU244
C	TYR6
C	GLU150
C	GLU156
C	ASP183
C	HIS209
A	GLU150
C	ARG215
C	GLU244
D	TYR6
D	GLU150
D	GLU156
D	ASP183
D	HIS209
D	ARG215
D	GLU244
A	GLU156
A	ASP183
A	HIS209
A	ARG215
A	GLU244
B	TYR6
B	GLU150

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:A9CH28

Chain	Residue	Details
A	ALA107
B	ALA107
C	ALA107
D	ALA107

---