3VNL

Crystal structures of D-Psicose 3-epimerase with D-tagatose 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	11
Details	BINDING SITE FOR RESIDUE TAG A 7101

Chain	Residue
A	TYR6
A	PHE246
A	MN7102
A	HIS66
A	GLY106
A	GLU150
A	GLU156
A	ASP183
A	HIS186
A	ARG215
A	GLU244

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 7102

Chain	Residue
A	GLU150
A	ASP183
A	HIS209
A	GLU244
A	TAG7101

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE TAG B 301

Chain	Residue
B	TYR6
B	TRP14
B	HIS66
B	GLU150
B	GLU156
B	ASP183
B	HIS186
B	HIS209
B	ARG215
B	GLU244
B	PHE246
B	ILE257
B	MN302

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN B 302

Chain	Residue
B	GLU150
B	ASP183
B	HIS209
B	GLU244
B	TAG301

---

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE TAG C 301

Chain	Residue
C	TYR6
C	HIS66
C	GLY67
C	GLY106
C	GLU150
C	GLU156
C	ASP183
C	HIS186
C	HIS209
C	ARG215
C	GLU244
C	MN302
C	HOH488

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 302

Chain	Residue
C	GLU150
C	ASP183
C	HIS209
C	GLU244
C	TAG301

---

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE TAG D 301

Chain	Residue
D	TYR6
D	TRP14
D	HIS66
D	GLY67
D	GLU150
D	LEU152
D	GLU156
D	ASP183
D	HIS186
D	ARG215
D	GLU244
D	MN302

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN D 302

Chain	Residue
D	GLU150
D	ASP183
D	HIS209
D	GLU244
D	TAG301

---

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

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