Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3CT7

Crystal structure of D-allulose 6-phosphate 3-epimerase from Escherichia Coli K-12

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004750	molecular_function	D-ribulose-phosphate 3-epimerase activity
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
A	0016853	molecular_function	isomerase activity
A	0016857	molecular_function	racemase and epimerase activity, acting on carbohydrates and derivatives
A	0019316	biological_process	D-allose catabolic process
A	0034700	molecular_function	allulose 6-phosphate 3-epimerase activity
A	0046872	molecular_function	metal ion binding
B	0004750	molecular_function	D-ribulose-phosphate 3-epimerase activity
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
B	0016853	molecular_function	isomerase activity
B	0016857	molecular_function	racemase and epimerase activity, acting on carbohydrates and derivatives
B	0019316	biological_process	D-allose catabolic process
B	0034700	molecular_function	allulose 6-phosphate 3-epimerase activity
B	0046872	molecular_function	metal ion binding
C	0004750	molecular_function	D-ribulose-phosphate 3-epimerase activity
C	0005829	cellular_component	cytosol
C	0005975	biological_process	carbohydrate metabolic process
C	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
C	0016853	molecular_function	isomerase activity
C	0016857	molecular_function	racemase and epimerase activity, acting on carbohydrates and derivatives
C	0019316	biological_process	D-allose catabolic process
C	0034700	molecular_function	allulose 6-phosphate 3-epimerase activity
C	0046872	molecular_function	metal ion binding
D	0004750	molecular_function	D-ribulose-phosphate 3-epimerase activity
D	0005829	cellular_component	cytosol
D	0005975	biological_process	carbohydrate metabolic process
D	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
D	0016853	molecular_function	isomerase activity
D	0016857	molecular_function	racemase and epimerase activity, acting on carbohydrates and derivatives
D	0019316	biological_process	D-allose catabolic process
D	0034700	molecular_function	allulose 6-phosphate 3-epimerase activity
D	0046872	molecular_function	metal ion binding
E	0004750	molecular_function	D-ribulose-phosphate 3-epimerase activity
E	0005829	cellular_component	cytosol
E	0005975	biological_process	carbohydrate metabolic process
E	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
E	0016853	molecular_function	isomerase activity
E	0016857	molecular_function	racemase and epimerase activity, acting on carbohydrates and derivatives
E	0019316	biological_process	D-allose catabolic process
E	0034700	molecular_function	allulose 6-phosphate 3-epimerase activity
E	0046872	molecular_function	metal ion binding
F	0004750	molecular_function	D-ribulose-phosphate 3-epimerase activity
F	0005829	cellular_component	cytosol
F	0005975	biological_process	carbohydrate metabolic process
F	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
F	0016853	molecular_function	isomerase activity
F	0016857	molecular_function	racemase and epimerase activity, acting on carbohydrates and derivatives
F	0019316	biological_process	D-allose catabolic process
F	0034700	molecular_function	allulose 6-phosphate 3-epimerase activity
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 232

Chain	Residue
A	HIS30
A	ASP32
A	HIS63
A	ASP173

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 233

Chain	Residue
A	SER197
A	ALA142
A	GLY143
A	SER175
A	GLY195
A	THR196

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 232

Chain	Residue
B	HIS30
B	ASP32
B	HIS63
B	ASP173

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 233

Chain	Residue
B	ALA142
B	GLY143
B	GLY195
B	THR196
B	SER197

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 301

Chain	Residue
C	HIS30
C	ASP32
C	HIS63
C	ASP173

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 302

Chain	Residue
C	ALA142
C	GLY143
C	SER175
C	GLY195
C	THR196
C	SER197

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 401

Chain	Residue
D	HIS30
D	ASP32
D	HIS63
D	ASP173

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 402

Chain	Residue
D	ALA142
D	GLY143
D	SER175
D	GLY195
D	THR196
D	SER197

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 501

Chain	Residue
E	HIS30
E	ASP32
E	HIS63
E	ASP173

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 502

Chain	Residue
E	ALA142
E	GLY143
E	SER175
E	GLY195
E	THR196
E	SER197

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG F 601

Chain	Residue
F	HIS30
F	ASP32
F	HIS63
F	ASP173

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 F 602

Chain	Residue
F	ALA142
F	GLY143
F	THR196
F	SER197

Functional Information from PROSITE/UniProt

site_id	PS01085
Number of Residues	15
Details	RIBUL_P_3_EPIMER_1 Ribulose-phosphate 3-epimerase family signature 1. FHIDImDghFVpNlT

Chain	Residue	Details
A	PHE29-THR43

site_id	PS01086
Number of Residues	23
Details	RIBUL_P_3_EPIMER_2 Ribulose-phosphate 3-epimerase family signature 2. ItVMTVdPgfaGQpFipemldKL

Chain	Residue	Details
A	ILE132-LEU154

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_02226","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18700786","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CTL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_02226","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18700786","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CTL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	54
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02226","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18700786","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CTL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02226","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18700786","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CT7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CTL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1rpx

Chain	Residue	Details
A	HIS30
A	ASP32
A	ASP173
A	HIS63

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1rpx

Chain	Residue	Details
B	HIS30
B	ASP32
B	ASP173
B	HIS63

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1rpx

Chain	Residue	Details
C	HIS30
C	ASP32
C	ASP173
C	HIS63

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1rpx

Chain	Residue	Details
D	HIS30
D	ASP32
D	ASP173
D	HIS63

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1rpx

Chain	Residue	Details
E	HIS30
E	ASP32
E	ASP173
E	HIS63

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1rpx

Chain	Residue	Details
F	HIS30
F	ASP32
F	ASP173
F	HIS63

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)