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6N9M

Crystal Structure of Adenosine Deaminase from Salmonella typhimurium with Pentostatin (Deoxycoformycin)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004000molecular_functionadenosine deaminase activity
A0005829cellular_componentcytosol
A0006154biological_processadenosine catabolic process
A0008270molecular_functionzinc ion binding
A0009117biological_processnucleotide metabolic process
A0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
A0009897cellular_componentexternal side of plasma membrane
A0016787molecular_functionhydrolase activity
A0019239molecular_functiondeaminase activity
A0043103biological_processhypoxanthine salvage
A0046103biological_processinosine biosynthetic process
A0046872molecular_functionmetal ion binding
A0046936molecular_function2'-deoxyadenosine deaminase activity
A0060169biological_processnegative regulation of adenosine receptor signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue DCF A 401
ChainResidue
AHIS12
AHIS197
AGLU200
AHIS221
AASP278
AASP279
AZN402
AHOH523
AHIS14
AASP16
ALEU56
ALEU60
AILE139
ASER141
AALA169
AGLY170

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 402
ChainResidue
AHIS12
AHIS14
AHIS197
AASP278
ADCF401

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 403
ChainResidue
AGLU117
AGLU328
AHOH568
AHOH667
AHOH676

site_idAC4
Number of Residues5
Detailsbinding site for residue CA A 404
ChainResidue
AGLY131
AGLU133
AGLU161
AHOH611
AHOH675

site_idAC5
Number of Residues2
Detailsbinding site for residue FMT A 405
ChainResidue
AARG29
AASN32

Functional Information from PROSITE/UniProt
site_idPS00485
Number of Residues7
DetailsA_DEAMINASE Adenosine and AMP deaminase signature. SLNTDDP
ChainResidueDetails
ASER274-PRO280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00540
ChainResidueDetails
AGLU200

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00540, ECO:0000269|Ref.2, ECO:0007744|PDB:6N9M
ChainResidueDetails
AHIS12
AHIS14
AHIS197
AASP278

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00540
ChainResidueDetails
AASP16
AGLY170
AASP279

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|Ref.2, ECO:0007744|PDB:6N9M
ChainResidueDetails
ASER141
AGLU200
AHIS221

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00540
ChainResidueDetails
AHIS221

218853

PDB entries from 2024-04-24

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