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4BMZ

Structure of futalosine hydrolase mutant of Helicobacter pylori strain 26695

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
A0009234biological_processmenaquinone biosynthetic process
A0016787molecular_functionhydrolase activity
A0019284biological_processL-methionine salvage from S-adenosylmethionine
A0019509biological_processL-methionine salvage from methylthioadenosine
A0102246molecular_function6-amino-6-deoxyfutalosine hydrolase activity
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
B0009234biological_processmenaquinone biosynthetic process
B0016787molecular_functionhydrolase activity
B0019284biological_processL-methionine salvage from S-adenosylmethionine
B0019509biological_processL-methionine salvage from methylthioadenosine
B0102246molecular_function6-amino-6-deoxyfutalosine hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE MTA A 1232
ChainResidue
AALA10
AGLU174
AMET175
AGLU176
AASN199
AALA201
APHE209
AHOH2003
BLEU105
AILE53
AVAL79
AALA80
AGLY81
AGLN153
APHE154
AVAL155
AVAL173

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE MTA B 1232
ChainResidue
ALEU105
APHE108
BHIS0
BALA10
BVAL79
BALA80
BGLY81
BGLN153
BPHE154
BVAL155
BGLU174
BMET175
BGLU176
BARG195
BASN199
BPHE209
BHOH2007

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AGLU14
BGLU14

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
AASN199
BASN199

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AGLY81
AVAL155
AMET175
BGLY81
BVAL155
BMET175

222415

PDB entries from 2024-07-10

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