Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3BSF

Crystal Structure of the MTA/SAH nucleosidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000003biological_processobsolete reproduction
A0003824molecular_functioncatalytic activity
A0008782molecular_functionadenosylhomocysteine nucleosidase activity
A0008930molecular_functionmethylthioadenosine nucleosidase activity
A0009086biological_processmethionine biosynthetic process
A0009116biological_processnucleoside metabolic process
A0010087biological_processphloem or xylem histogenesis
A0016787molecular_functionhydrolase activity
A0019509biological_processL-methionine salvage from methylthioadenosine
B0000003biological_processobsolete reproduction
B0003824molecular_functioncatalytic activity
B0008782molecular_functionadenosylhomocysteine nucleosidase activity
B0008930molecular_functionmethylthioadenosine nucleosidase activity
B0009086biological_processmethionine biosynthetic process
B0009116biological_processnucleoside metabolic process
B0010087biological_processphloem or xylem histogenesis
B0016787molecular_functionhydrolase activity
B0019509biological_processL-methionine salvage from methylthioadenosine
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ADE A 701
ChainResidue
AMET168
ALYS186
ATHR211
AASP212
AHOH704

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ADE B 702
ChainResidue
BASP187
BTHR211
BASP212
BVAL214
BPHE224
BHOH707
BALA104
BGLY105
BMET168
BLYS186

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q9T0I8
ChainResidueDetails
AGLU25
BGLU25

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q9T0I8
ChainResidueDetails
AASP212
BASP212

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9T0I8
ChainResidueDetails
ATHR103
BTHR103

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19249293
ChainResidueDetails
ALYS186
AASP212
BLYS186
BASP212

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895
ChainResidueDetails
AMET1
BMET1

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon