Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1EZR

CRYSTAL STRUCTURE OF NUCLEOSIDE HYDROLASE FROM LEISHMANIA MAJOR

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
A	0005575	cellular_component	cellular_component
A	0005829	cellular_component	cytosol
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006152	biological_process	purine nucleoside catabolic process
A	0008477	molecular_function	purine nucleosidase activity
A	0009117	biological_process	nucleotide metabolic process
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
A	0043101	biological_process	purine-containing compound salvage
A	0045437	molecular_function	uridine nucleosidase activity
A	0046872	molecular_function	metal ion binding
A	0047724	molecular_function	inosine nucleosidase activity
B	0005509	molecular_function	calcium ion binding
B	0005575	cellular_component	cellular_component
B	0005829	cellular_component	cytosol
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0006152	biological_process	purine nucleoside catabolic process
B	0008477	molecular_function	purine nucleosidase activity
B	0009117	biological_process	nucleotide metabolic process
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
B	0043101	biological_process	purine-containing compound salvage
B	0045437	molecular_function	uridine nucleosidase activity
B	0046872	molecular_function	metal ion binding
B	0047724	molecular_function	inosine nucleosidase activity
C	0005509	molecular_function	calcium ion binding
C	0005575	cellular_component	cellular_component
C	0005829	cellular_component	cytosol
C	0006139	biological_process	nucleobase-containing compound metabolic process
C	0006152	biological_process	purine nucleoside catabolic process
C	0008477	molecular_function	purine nucleosidase activity
C	0009117	biological_process	nucleotide metabolic process
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
C	0043101	biological_process	purine-containing compound salvage
C	0045437	molecular_function	uridine nucleosidase activity
C	0046872	molecular_function	metal ion binding
C	0047724	molecular_function	inosine nucleosidase activity
D	0005509	molecular_function	calcium ion binding
D	0005575	cellular_component	cellular_component
D	0005829	cellular_component	cytosol
D	0006139	biological_process	nucleobase-containing compound metabolic process
D	0006152	biological_process	purine nucleoside catabolic process
D	0008477	molecular_function	purine nucleosidase activity
D	0009117	biological_process	nucleotide metabolic process
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
D	0043101	biological_process	purine-containing compound salvage
D	0045437	molecular_function	uridine nucleosidase activity
D	0046872	molecular_function	metal ion binding
D	0047724	molecular_function	inosine nucleosidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 401

Chain	Residue
A	ASP10
A	ASP15
A	THR126
A	ASP241

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 401

Chain	Residue
B	ASP10
B	ASP15
B	THR126
B	ASP241

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA C 401

Chain	Residue
C	ASP15
C	THR126
C	ASP241
C	ASP10

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA D 401

Chain	Residue
D	ASP10
D	ASP15
D	THR126
D	ASP241

Functional Information from PROSITE/UniProt

site_id	PS01247
Number of Residues	11
Details	IUNH Inosine-uridine preferring nucleoside hydrolase family signature. DcDPGiDDAVA

Chain	Residue	Details
A	ASP8-ALA18

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000250\|UniProtKB:Q27546

Chain	Residue	Details
A	ASP241
B	ASP241
C	ASP241
D	ASP241

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING:

Chain	Residue	Details
A	PRO11
C	ALA16
C	GLY127
C	PRO242
D	PRO11
D	ALA16
D	GLY127
D	PRO242
A	ALA16
A	GLY127
A	PRO242
B	PRO11
B	ALA16
B	GLY127
B	PRO242
C	PRO11

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ASP15
C	ALA161
C	PHE167
C	VAL169
D	ASP15
D	ALA161
D	PHE167
D	VAL169
A	ALA161
A	PHE167
A	VAL169
B	ASP15
B	ALA161
B	PHE167
B	VAL169
C	ASP15

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1mas

Chain	Residue	Details
A	ASP10
A	HIS240
A	ASN168

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1mas

Chain	Residue	Details
B	ASP10
B	HIS240
B	ASN168

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1mas

Chain	Residue	Details
C	ASP10
C	HIS240
C	ASN168

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1mas

Chain	Residue	Details
D	ASP10
D	HIS240
D	ASN168

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)