Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1JDI

CRYSTAL STRUCTURE OF L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005829	cellular_component	cytosol
A	0005996	biological_process	monosaccharide metabolic process
A	0008270	molecular_function	zinc ion binding
A	0008742	molecular_function	L-ribulose-phosphate 4-epimerase activity
A	0016832	molecular_function	aldehyde-lyase activity
A	0016853	molecular_function	isomerase activity
A	0019323	biological_process	pentose catabolic process
A	0019324	biological_process	L-lyxose metabolic process
A	0019568	biological_process	arabinose catabolic process
A	0019569	biological_process	L-arabinose catabolic process to D-xylulose 5-phosphate
A	0019572	biological_process	L-arabinose catabolic process
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
B	0005829	cellular_component	cytosol
B	0005996	biological_process	monosaccharide metabolic process
B	0008270	molecular_function	zinc ion binding
B	0008742	molecular_function	L-ribulose-phosphate 4-epimerase activity
B	0016832	molecular_function	aldehyde-lyase activity
B	0016853	molecular_function	isomerase activity
B	0019323	biological_process	pentose catabolic process
B	0019324	biological_process	L-lyxose metabolic process
B	0019568	biological_process	arabinose catabolic process
B	0019569	biological_process	L-arabinose catabolic process to D-xylulose 5-phosphate
B	0019572	biological_process	L-arabinose catabolic process
B	0032991	cellular_component	protein-containing complex
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
C	0005829	cellular_component	cytosol
C	0005996	biological_process	monosaccharide metabolic process
C	0008270	molecular_function	zinc ion binding
C	0008742	molecular_function	L-ribulose-phosphate 4-epimerase activity
C	0016832	molecular_function	aldehyde-lyase activity
C	0016853	molecular_function	isomerase activity
C	0019323	biological_process	pentose catabolic process
C	0019324	biological_process	L-lyxose metabolic process
C	0019568	biological_process	arabinose catabolic process
C	0019569	biological_process	L-arabinose catabolic process to D-xylulose 5-phosphate
C	0019572	biological_process	L-arabinose catabolic process
C	0032991	cellular_component	protein-containing complex
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
D	0005829	cellular_component	cytosol
D	0005996	biological_process	monosaccharide metabolic process
D	0008270	molecular_function	zinc ion binding
D	0008742	molecular_function	L-ribulose-phosphate 4-epimerase activity
D	0016832	molecular_function	aldehyde-lyase activity
D	0016853	molecular_function	isomerase activity
D	0019323	biological_process	pentose catabolic process
D	0019324	biological_process	L-lyxose metabolic process
D	0019568	biological_process	arabinose catabolic process
D	0019569	biological_process	L-arabinose catabolic process to D-xylulose 5-phosphate
D	0019572	biological_process	L-arabinose catabolic process
D	0032991	cellular_component	protein-containing complex
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
E	0005829	cellular_component	cytosol
E	0005996	biological_process	monosaccharide metabolic process
E	0008270	molecular_function	zinc ion binding
E	0008742	molecular_function	L-ribulose-phosphate 4-epimerase activity
E	0016832	molecular_function	aldehyde-lyase activity
E	0016853	molecular_function	isomerase activity
E	0019323	biological_process	pentose catabolic process
E	0019324	biological_process	L-lyxose metabolic process
E	0019568	biological_process	arabinose catabolic process
E	0019569	biological_process	L-arabinose catabolic process to D-xylulose 5-phosphate
E	0019572	biological_process	L-arabinose catabolic process
E	0032991	cellular_component	protein-containing complex
E	0042802	molecular_function	identical protein binding
E	0046872	molecular_function	metal ion binding
F	0005829	cellular_component	cytosol
F	0005996	biological_process	monosaccharide metabolic process
F	0008270	molecular_function	zinc ion binding
F	0008742	molecular_function	L-ribulose-phosphate 4-epimerase activity
F	0016832	molecular_function	aldehyde-lyase activity
F	0016853	molecular_function	isomerase activity
F	0019323	biological_process	pentose catabolic process
F	0019324	biological_process	L-lyxose metabolic process
F	0019568	biological_process	arabinose catabolic process
F	0019569	biological_process	L-arabinose catabolic process to D-xylulose 5-phosphate
F	0019572	biological_process	L-arabinose catabolic process
F	0032991	cellular_component	protein-containing complex
F	0042802	molecular_function	identical protein binding
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	HIS95
A	HIS97
A	HIS171
A	HOH308

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN B 302

Chain	Residue
B	HIS95
B	HIS97
B	HIS171

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 303

Chain	Residue
C	HIS171
C	HOH312
C	HIS95
C	HIS97

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 304

Chain	Residue
D	HIS95
D	HIS97
D	HIS171
D	HOH402

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN E 305

Chain	Residue
E	HIS95
E	HIS97
E	HIS171

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN F 306

Chain	Residue
F	HIS95
F	HIS97
F	HIS171

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00989","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11732896","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P0AB87","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00989","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00989","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10769138","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9548961","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00989","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11732895","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11732896","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10769138","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"10769139","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1JDI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K0W","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00989","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11732895","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11732896","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10769138","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1JDI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K0W","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1k0w

Chain	Residue	Details
A	ASP120

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1k0w

Chain	Residue	Details
B	ASP120

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1k0w

Chain	Residue	Details
C	ASP120

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1k0w

Chain	Residue	Details
D	ASP120

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1k0w

Chain	Residue	Details
E	ASP120

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1k0w

Chain	Residue	Details
F	ASP120

site_id	MCSA1
Number of Residues	4
Details	M-CSA 273

Chain	Residue	Details
A	HIS95	metal ligand
A	HIS97	metal ligand
A	ASP120	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS171	metal ligand

site_id	MCSA2
Number of Residues	4
Details	M-CSA 273

Chain	Residue	Details
B	HIS95	metal ligand
B	HIS97	metal ligand
B	ASP120	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS171	metal ligand

site_id	MCSA3
Number of Residues	4
Details	M-CSA 273

Chain	Residue	Details
C	HIS95	metal ligand
C	HIS97	metal ligand
C	ASP120	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	HIS171	metal ligand

site_id	MCSA4
Number of Residues	4
Details	M-CSA 273

Chain	Residue	Details
D	HIS95	metal ligand
D	HIS97	metal ligand
D	ASP120	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	HIS171	metal ligand

site_id	MCSA5
Number of Residues	4
Details	M-CSA 273

Chain	Residue	Details
E	HIS95	metal ligand
E	HIS97	metal ligand
E	ASP120	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	HIS171	metal ligand

site_id	MCSA6
Number of Residues	4
Details	M-CSA 273

Chain	Residue	Details
F	HIS95	metal ligand
F	HIS97	metal ligand
F	ASP120	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	HIS171	metal ligand

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