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4BMX

Native structure of futalosine hydrolase of Helicobacter pylori strain 26695

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
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
B0008652biological_processamino acid biosynthetic process
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 Residues11
DetailsBINDING SITE FOR RESIDUE ADE B 1232
ChainResidue
BALA80
BALA201
BTRS1233
BGLY81
BPHE154
BVAL155
BVAL173
BGLU174
BMET175
BSER198
BASP199

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TRS B 1233
ChainResidue
BMET1
BALA10
BMET11
BGLU14
BVAL79
BGLU174
BMET175
BGLU176
BARG195
BPHE209
BADE1232

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE TRS A 1232
ChainResidue
ASER125
AGLU126
ASER127

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
AASP199
BASP199

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

218853

PDB entries from 2024-04-24

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