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1MAS

PURINE NUCLEOSIDE HYDROLASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006152biological_processpurine nucleoside catabolic process
A0008477molecular_functionpurine nucleosidase activity
A0009117biological_processnucleotide metabolic process
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
B0006139biological_processnucleobase-containing compound metabolic process
B0006152biological_processpurine nucleoside catabolic process
B0008477molecular_functionpurine nucleosidase activity
B0009117biological_processnucleotide metabolic process
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
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:8634238
ChainResidueDetails
AASP242
BASP242

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
APRO11
AALA16
AGLY127
APRO243
BPRO11
BALA16
BGLY127
BPRO243

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:8634238
ChainResidueDetails
AASP15
AALA161
APHE167
AILE169
BASP15
BALA161
BPHE167
BILE169

Catalytic Information from CSA
site_idMCSA1
Number of Residues8
DetailsM-CSA 39
ChainResidueDetails
APRO11hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
AALA16metal ligand
AGLN40metal ligand
AGLY127metal ligand
AASN168electrostatic stabiliser
AILE169electrostatic stabiliser, hydrogen bond donor
AASP242hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
APRO243metal ligand

site_idMCSA2
Number of Residues8
DetailsM-CSA 39
ChainResidueDetails
BPRO11hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
BALA16metal ligand
BGLN40metal ligand
BGLY127metal ligand
BASN168electrostatic stabiliser
BILE169electrostatic stabiliser, hydrogen bond donor
BASP242hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BPRO243metal ligand

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PDB entries from 2024-05-22

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