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1Z5O

Crystal structure of MTA/AdoHcy nucleosidase Asp197Asn mutant complexed with 5'-methylthioadenosine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008782molecular_functionadenosylhomocysteine nucleosidase activity
A0008930molecular_functionmethylthioadenosine nucleosidase activity
A0009086biological_processmethionine biosynthetic process
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0016787molecular_functionhydrolase activity
A0019284biological_processL-methionine salvage from S-adenosylmethionine
A0019509biological_processL-methionine salvage from methylthioadenosine
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046124biological_processpurine deoxyribonucleoside catabolic process
A0110052biological_processtoxic metabolite repair
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008782molecular_functionadenosylhomocysteine nucleosidase activity
B0008930molecular_functionmethylthioadenosine nucleosidase activity
B0009086biological_processmethionine biosynthetic process
B0009116biological_processnucleoside metabolic process
B0009164biological_processnucleoside catabolic process
B0016787molecular_functionhydrolase activity
B0019284biological_processL-methionine salvage from S-adenosylmethionine
B0019509biological_processL-methionine salvage from methylthioadenosine
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046124biological_processpurine deoxyribonucleoside catabolic process
B0110052biological_processtoxic metabolite repair
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE MTA A 5233
ChainResidue
ASER76
AARG193
AASN197
APHE207
AHOH5234
AHOH5277
AALA77
AGLY78
AALA150
APHE151
AILE152
AGLU172
AMET173
AGLU174

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE MTA B 9233
ChainResidue
BALA8
BILE50
BSER76
BALA77
BGLY78
BALA150
BPHE151
BILE152
BGLU172
BMET173
BGLU174
BARG193
BASN197
BPHE207
BHOH9243
BHOH9251

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000305|PubMed:16109423
ChainResidueDetails
AGLU12
BGLU12

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000305|PubMed:16109423
ChainResidueDetails
AASN197
BASN197

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000269|PubMed:11591349
ChainResidueDetails
AGLY78
AILE152
BGLY78
BILE152

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01684
ChainResidueDetails
AMET173
BMET173

226707

PDB entries from 2024-10-30

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