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 | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00540","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00540","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of adenosine deaminase from Vibrio cholerae complexed with pentostatin (deoxycoformycin) (CASP target).","authors":["Maltseva N.","Kim Y.","Endres M.","Welk L.","Joachimiak A."]}},{"source":"PDB","id":"6N91","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of adenosine deaminase from Vibrio cholerae complexed with pentostatin (deoxycoformycin) (CASP target).","authors":["Maltseva N.","Kim Y.","Endres M.","Welk L.","Joachimiak A."]}},{"source":"PDB","id":"6N91","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00540","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_00540","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
