4Z0V
The structure of human PDE12 residues 161-609
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 701 |
| Chain | Residue |
| A | GLU351 |
| A | HOH809 |
| A | HOH824 |
| A | HOH848 |
| A | HOH1008 |
| A | HOH1031 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 702 |
| Chain | Residue |
| A | GLY255 |
| A | ARG257 |
| A | PHE258 |
| A | HOH807 |
| A | SER192 |
| A | GLY253 |
| A | ASP254 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 703 |
| Chain | Residue |
| A | GLN396 |
| A | HIS397 |
| A | ASP398 |
| A | HOH861 |
| A | HOH876 |
| A | HOH904 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 704 |
| Chain | Residue |
| A | LEU393 |
| A | GLN396 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 705 |
| Chain | Residue |
| A | ASN568 |
| A | LYS609 |
| A | HOH803 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 706 |
| Chain | Residue |
| A | TRP459 |
| A | PRO461 |
| A | ARG467 |
| A | ASN498 |
| A | HOH1047 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 707 |
| Chain | Residue |
| A | LYS417 |
| A | LEU534 |
| A | THR535 |
| A | HOH922 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q96LI5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26055709","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2015","submissionDatabase":"PDB data bank","title":"Crystal structure of human phosphodiesterase.","authors":["Kim S.Y.","Kohno T.","Mori T.","Kitano K.","Hakoshima T."]}},{"source":"PDB","id":"4Z0V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ZKF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2015","submissionDatabase":"PDB data bank","title":"Crystal structure of human phosphodiesterase.","authors":["Kim S.Y.","Kohno T.","Mori T.","Kitano K.","Hakoshima T."]}},{"source":"PDB","id":"4ZKF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
