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1MAS

PURINE NUCLEOSIDE HYDROLASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0006152biological_processpurine nucleoside catabolic process
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
A0045437molecular_functionuridine nucleosidase activity
A0046872molecular_functionmetal ion binding
A0047724molecular_functioninosine nucleosidase activity
B0005829cellular_componentcytosol
B0006152biological_processpurine nucleoside catabolic process
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
B0045437molecular_functionuridine nucleosidase activity
B0046872molecular_functionmetal ion binding
B0047724molecular_functioninosine nucleosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 900
ChainResidue
AASP10
AASP15
ATHR126
AASP242
AHOH902

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K B 933
ChainResidue
BASP10
BASP15
BTHR126
BASP242

site_idACT
Number of Residues10
DetailsPOCKET AT THE C-TERMINAL END OF THE BETA SHEET.
ChainResidue
AASP10
BASP242
AASP14
AASP15
AHIS241
AASP242
BASP10
BASP14
BASP15
BHIS241

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"8634238","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8634238","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 9572842, 8634238, 8634237, 12137535
ChainResidueDetails
AASP10
AHIS241
AASN168

site_idCSA2
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 9572842, 8634238, 8634237, 12137535
ChainResidueDetails
BASP10
BHIS241
BASN168

site_idMCSA1
Number of Residues8
DetailsM-CSA 39
ChainResidueDetails
AASP10hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
AASP15metal ligand
AASN39metal ligand
ATHR126metal ligand
APHE167electrostatic stabiliser
AASN168electrostatic stabiliser, hydrogen bond donor
AHIS241hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASP242metal ligand

site_idMCSA2
Number of Residues8
DetailsM-CSA 39
ChainResidueDetails
BASP10hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
BASP15metal ligand
BASN39metal ligand
BTHR126metal ligand
BPHE167electrostatic stabiliser
BASN168electrostatic stabiliser, hydrogen bond donor
BHIS241hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BASP242metal ligand

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PDB entries from 2025-12-24

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