6N91
Crystal Structure of Adenosine Deaminase from Vibrio cholerae Complexed with Pentostatin (Deoxycoformycin)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004000 | molecular_function | adenosine deaminase activity |
A | 0005829 | cellular_component | cytosol |
A | 0006154 | biological_process | adenosine catabolic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0009117 | biological_process | nucleotide metabolic process |
A | 0009168 | biological_process | purine ribonucleoside monophosphate biosynthetic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019239 | molecular_function | deaminase activity |
A | 0043103 | biological_process | hypoxanthine salvage |
A | 0046103 | biological_process | inosine biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0046936 | molecular_function | 2'-deoxyadenosine deaminase activity |
B | 0004000 | molecular_function | adenosine deaminase activity |
B | 0005829 | cellular_component | cytosol |
B | 0006154 | biological_process | adenosine catabolic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0009117 | biological_process | nucleotide metabolic process |
B | 0009168 | biological_process | purine ribonucleoside monophosphate biosynthetic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0019239 | molecular_function | deaminase activity |
B | 0043103 | biological_process | hypoxanthine salvage |
B | 0046103 | biological_process | inosine biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0046936 | molecular_function | 2'-deoxyadenosine deaminase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | binding site for residue DCF A 401 |
Chain | Residue |
A | HIS12 |
A | HIS197 |
A | GLU200 |
A | HIS221 |
A | ASP278 |
A | ASP279 |
A | ZN402 |
A | HOH510 |
A | HIS14 |
A | ASP16 |
A | LEU56 |
A | LEU60 |
A | ILE139 |
A | SER141 |
A | ALA169 |
A | GLY170 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue ZN A 402 |
Chain | Residue |
A | HIS12 |
A | HIS14 |
A | HIS197 |
A | ASP278 |
A | DCF401 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue CXS A 403 |
Chain | Residue |
A | TYR94 |
A | VAL123 |
A | ARG124 |
A | GLN133 |
A | ALA134 |
A | ASN135 |
A | HIS162 |
A | SO4405 |
A | PO4406 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue FMT A 404 |
Chain | Residue |
A | VAL112 |
A | THR113 |
A | GLN151 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 405 |
Chain | Residue |
A | ASN135 |
A | ASN161 |
A | CXS403 |
A | PO4406 |
A | HOH641 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue PO4 A 406 |
Chain | Residue |
A | ARG124 |
A | CXS403 |
A | SO4405 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue GOL A 407 |
Chain | Residue |
A | HIS162 |
site_id | AC8 |
Number of Residues | 15 |
Details | binding site for residue DCF B 401 |
Chain | Residue |
B | HIS14 |
B | ASP16 |
B | LEU56 |
B | LEU60 |
B | ILE139 |
B | SER141 |
B | ALA169 |
B | GLY170 |
B | HIS197 |
B | GLU200 |
B | HIS221 |
B | ASP278 |
B | ASP279 |
B | ZN402 |
B | HOH555 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue ZN B 402 |
Chain | Residue |
B | HIS12 |
B | HIS14 |
B | HIS197 |
B | ASP278 |
B | DCF401 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue CXS B 403 |
Chain | Residue |
B | VAL123 |
B | ARG124 |
B | GLN133 |
B | ALA134 |
B | ASN135 |
B | HIS162 |
B | PO4408 |
B | CXS409 |
site_id | AD2 |
Number of Residues | 1 |
Details | binding site for residue FMT B 404 |
Chain | Residue |
B | SER4 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue NA B 405 |
Chain | Residue |
A | GLN48 |
A | HOH542 |
A | HOH579 |
B | GLN48 |
B | ILE49 |
B | HOH613 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue EDO B 406 |
Chain | Residue |
B | PRO111 |
B | VAL112 |
B | THR113 |
B | GLN151 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue GOL B 407 |
Chain | Residue |
B | GLY145 |
B | THR146 |
B | ASP147 |
B | GLN175 |
B | HOH553 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue PO4 B 408 |
Chain | Residue |
B | ARG124 |
B | HIS162 |
B | CXS403 |
B | CXS409 |
site_id | AD7 |
Number of Residues | 10 |
Details | binding site for residue CXS B 409 |
Chain | Residue |
B | HOH525 |
B | ASN135 |
B | LYS160 |
B | ASN161 |
B | ILE163 |
B | ALA190 |
B | GLY191 |
B | LEU192 |
B | CXS403 |
B | PO4408 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00540 |
Chain | Residue | Details |
A | GLU200 | |
B | GLU200 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00540, ECO:0000269|Ref.2, ECO:0007744|PDB:6N91 |
Chain | Residue | Details |
A | HIS12 | |
A | HIS14 | |
A | HIS197 | |
A | ASP278 | |
B | HIS12 | |
B | HIS14 | |
B | HIS197 | |
B | ASP278 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00540 |
Chain | Residue | Details |
A | ASP16 | |
A | GLY170 | |
A | ASP279 | |
B | ASP16 | |
B | GLY170 | |
B | ASP279 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|Ref.2, ECO:0007744|PDB:6N91 |
Chain | Residue | Details |
A | SER141 | |
A | GLU200 | |
A | HIS221 | |
B | SER141 | |
B | GLU200 | |
B | HIS221 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00540 |
Chain | Residue | Details |
A | HIS221 | |
B | HIS221 |