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4QEZ

Crystal structure of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Bacillus anthracis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0008782molecular_functionadenosylhomocysteine nucleosidase activity
A0008930molecular_functionmethylthioadenosine nucleosidase activity
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0019284biological_processL-methionine salvage from S-adenosylmethionine
A0019509biological_processL-methionine salvage from methylthioadenosine
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0008782molecular_functionadenosylhomocysteine nucleosidase activity
B0008930molecular_functionmethylthioadenosine nucleosidase activity
B0009116biological_processnucleoside metabolic process
B0009164biological_processnucleoside catabolic process
B0019284biological_processL-methionine salvage from S-adenosylmethionine
B0019509biological_processL-methionine salvage from methylthioadenosine
C0003824molecular_functioncatalytic activity
C0005829cellular_componentcytosol
C0008782molecular_functionadenosylhomocysteine nucleosidase activity
C0008930molecular_functionmethylthioadenosine nucleosidase activity
C0009116biological_processnucleoside metabolic process
C0009164biological_processnucleoside catabolic process
C0019284biological_processL-methionine salvage from S-adenosylmethionine
C0019509biological_processL-methionine salvage from methylthioadenosine
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ADE B 301
ChainResidue
BALA77
BGLY78
BPHE152
BMET153
BVAL172
BGLU173
BSER197
BASP198
BTRS302

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRS B 302
ChainResidue
BALA8
BGLU12
BSER76
BGLU173
BMET174
BGLU175
BARG194
BADE301
CHIS236

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ADE A 301
ChainResidue
AALA77
AGLY78
APHE152
AMET153
AVAL172
AGLU173
ASER197
AASP198
ATRS302

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TRS A 302
ChainResidue
AALA8
AGLU12
ASER76
AGLU173
AMET174
AGLU175
AARG194
APHE208
AADE301
BHIS236

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRS C 301
ChainResidue
CALA8
CGLU12
CSER76
CGLU173
CMET174
CGLU175
CARG194
CPHE208
CADE302

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ADE C 302
ChainResidue
CALA77
CGLY78
CPHE152
CMET153
CVAL172
CGLU173
CSER197
CASP198
CPHE208
CTRS301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01684","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01684","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01684","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2026-04-01

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