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4G89

Crystal structure of k. pneumoniae mta/adohcy nucleosidase in complex with fragmented s-adenosyl-l-homocysteine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
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
A0046124biological_processpurine deoxyribonucleoside catabolic process
B0003824molecular_functioncatalytic activity
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
B0046124biological_processpurine deoxyribonucleoside catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ADE A 301
ChainResidue
AALA77
ASAH302
AGLY78
AALA150
APHE151
AILE152
AGLU172
ASER196
AASP197
AALA199

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE SAH A 302
ChainResidue
AALA8
AMET9
AILE50
ASER76
AALA135
ALEU136
APHE151
AGLU172
AMET173
AGLU174
AARG193
APHE207
AADE301
AHOH460
BPHE105
BTYR107
BPRO113

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AGLY154
ASER155
ALEU158
AASP200
AGLN201
AHOH535

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

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01684
ChainResidueDetails
AASP197
BASP197

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01684
ChainResidueDetails
AMET173
BGLY78
BILE152
BMET173
AGLY78
AILE152

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PDB entries from 2024-06-12

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