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1EZR

CRYSTAL STRUCTURE OF NUCLEOSIDE HYDROLASE FROM LEISHMANIA MAJOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0008477molecular_functionpurine nucleosidase activity
A0009117biological_processnucleotide metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
A0043101biological_processpurine-containing compound salvage
A0045437molecular_functionuridine nucleosidase activity
A0046872molecular_functionmetal ion binding
A0047724molecular_functioninosine nucleosidase activity
B0005509molecular_functioncalcium ion binding
B0008477molecular_functionpurine nucleosidase activity
B0009117biological_processnucleotide metabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
B0043101biological_processpurine-containing compound salvage
B0045437molecular_functionuridine nucleosidase activity
B0046872molecular_functionmetal ion binding
B0047724molecular_functioninosine nucleosidase activity
C0005509molecular_functioncalcium ion binding
C0008477molecular_functionpurine nucleosidase activity
C0009117biological_processnucleotide metabolic process
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
C0043101biological_processpurine-containing compound salvage
C0045437molecular_functionuridine nucleosidase activity
C0046872molecular_functionmetal ion binding
C0047724molecular_functioninosine nucleosidase activity
D0005509molecular_functioncalcium ion binding
D0008477molecular_functionpurine nucleosidase activity
D0009117biological_processnucleotide metabolic process
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
D0043101biological_processpurine-containing compound salvage
D0045437molecular_functionuridine nucleosidase activity
D0046872molecular_functionmetal ion binding
D0047724molecular_functioninosine nucleosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASP10
AASP15
ATHR126
AASP241

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 401
ChainResidue
BASP10
BASP15
BTHR126
BASP241

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C 401
ChainResidue
CASP15
CTHR126
CASP241
CASP10

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA D 401
ChainResidue
DASP10
DASP15
DTHR126
DASP241

Functional Information from PROSITE/UniProt
site_idPS01247
Number of Residues11
DetailsIUNH Inosine-uridine preferring nucleoside hydrolase family signature. DcDPGiDDAVA
ChainResidueDetails
AASP8-ALA18

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q27546","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1mas
ChainResidueDetails
AASP10
AHIS240
AASN168

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1mas
ChainResidueDetails
BASP10
BHIS240
BASN168

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1mas
ChainResidueDetails
CASP10
CHIS240
CASN168

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1mas
ChainResidueDetails
DASP10
DHIS240
DASN168

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PDB entries from 2025-07-23

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