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2QVN

Crystal structure of adenosine deaminase from Plasmodium vivax in complex with guanosine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004000molecular_functionadenosine deaminase activity
A0005829cellular_componentcytosol
A0006154biological_processadenosine catabolic process
A0006166biological_processpurine ribonucleoside salvage
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
A0090614molecular_function5'-methylthioadenosine deaminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GMP A 500
ChainResidue
AHIS44
AHIS253
ASER280
AASP310
AASP311
AHOH601
AHOH680
AASP46
ALEU85
APHE88
AILE170
AASP172
AGLY201
AHIS226
AGLU229

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NHE A 600
ChainResidue
AHIS161
AHIS164

Functional Information from PROSITE/UniProt
site_idPS00485
Number of Residues7
DetailsA_DEAMINASE Adenosine and AMP deaminase signature. SVNSDDP
ChainResidueDetails
ASER306-PRO312

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:18602399, ECO:0000269|PubMed:19728741, ECO:0007744|PDB:2PGF, ECO:0007744|PDB:2PGR, ECO:0007744|PDB:3EWC, ECO:0007744|PDB:3EWD
ChainResidueDetails
AHIS42
AHIS44
AHIS226
AHIS253
AASP310

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18602399, ECO:0000269|PubMed:19728741, ECO:0007744|PDB:2PGF, ECO:0007744|PDB:2PGR, ECO:0007744|PDB:2QVN, ECO:0007744|PDB:3EWC
ChainResidueDetails
AASP172

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18602399, ECO:0000269|PubMed:19728741, ECO:0007744|PDB:2PGF, ECO:0007744|PDB:2PGR, ECO:0007744|PDB:2QVN, ECO:0007744|PDB:3EWD
ChainResidueDetails
AGLY201

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18602399, ECO:0000269|PubMed:19728741, ECO:0007744|PDB:2PGF, ECO:0007744|PDB:2PGR, ECO:0007744|PDB:2QVN, ECO:0007744|PDB:3EWC, ECO:0007744|PDB:3EWD
ChainResidueDetails
AGLU229

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Important for substrate specificity for S-methyl-5'-thioadenosine => ECO:0000269|PubMed:19728741
ChainResidueDetails
AASP172

221371

PDB entries from 2024-06-19

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