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1V7A

Crystal structures of adenosine deaminase complexed with potent inhibitors

Functional Information from GO Data
ChainGOidnamespacecontents
A0004000molecular_functionadenosine deaminase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006154biological_processadenosine catabolic process
A0007155biological_processcell adhesion
A0008270molecular_functionzinc ion binding
A0009117biological_processnucleotide metabolic process
A0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
A0009897cellular_componentexternal side of plasma membrane
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019239molecular_functiondeaminase activity
A0031410cellular_componentcytoplasmic vesicle
A0042110biological_processT cell activation
A0043103biological_processhypoxanthine salvage
A0046103biological_processinosine biosynthetic process
A0046872molecular_functionmetal ion binding
A0046936molecular_function2'-deoxyadenosine deaminase activity
A0060169biological_processnegative regulation of adenosine receptor signaling pathway
A0060205cellular_componentcytoplasmic vesicle lumen
A0070161cellular_componentanchoring junction
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
AHIS15
AHIS17
AHIS214
AASP295
AHOH1039

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FRC A 1001
ChainResidue
APHE65
ATYR102
ASER103
ALEU106
ATRP117
AMET155
AALA183
AGLY184
AASP185
AASP296
AHOH1023
AHOH1171
AHIS17
AASP19
APHE61
ALEU62

Functional Information from PROSITE/UniProt
site_idPS00485
Number of Residues7
DetailsA_DEAMINASE Adenosine and AMP deaminase signature. SLNTDDP
ChainResidueDetails
ASER291-PRO297

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P03958
ChainResidueDetails
AVAL218

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL
ChainResidueDetails
AVAL16
ALEU18
AALA215
AASP296

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL
ChainResidueDetails
AGLY20

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:16060665, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1WXY
ChainResidueDetails
AASP185

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL
ChainResidueDetails
APRO297

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813
ChainResidueDetails
APRO59
AALA63

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000250|UniProtKB:P03958
ChainResidueDetails
AGLY239

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P00813
ChainResidueDetails
AGLN3

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00813
ChainResidueDetails
APRO55
ATHR233

218853

PDB entries from 2024-04-24

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