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6II7

Crystal structure of Plasmodium falciparum adenosine deaminase C27Q+L227I mutant co-complexed with Zn ion, hypoxanthine and inosine

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
A0060169biological_processnegative regulation of adenosine receptor signaling pathway
A0090614molecular_function5'-methylthioadenosine deaminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue NOS A 401
ChainResidue
AHIS48
AALA204
AGLY205
AASP315
AMET318
AHPA402
AHOH501
AHOH505
AHOH513
AHOH560
AASP50
AVAL51
AALA96
ASER133
APHE136
ATHR174
AGLY175
AASP176

site_idAC2
Number of Residues10
Detailsbinding site for residue HPA A 402
ChainResidue
AHIS48
ALEU89
AVAL93
AGLY205
AGLU233
AHIS257
AASP314
AASP315
ANOS401
AZN403

site_idAC3
Number of Residues5
Detailsbinding site for residue ZN A 403
ChainResidue
AHIS46
AHIS48
AHIS230
AASP314
AHPA402

site_idAC4
Number of Residues5
Detailsbinding site for residue ZN A 404
ChainResidue
AASP144
AASP146
AASP295
AHIS333
AHOH544

Functional Information from PROSITE/UniProt
site_idPS00485
Number of Residues7
DetailsA_DEAMINASE Adenosine and AMP deaminase signature. SVNSDDP
ChainResidueDetails
ASER310-PRO316

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsRegion: {"description":"Gating helix loop; regulates binding affinity for substrates and thus substrate selectivity","evidences":[{"source":"PubMed","id":"31002765","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31002765","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6II7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"A5KE01","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31002765","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6II7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Important for substrate specificity for S-methyl-5'-thioadenosine","evidences":[{"source":"UniProtKB","id":"A5KE01","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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