2D8A
Crystal Structure of PH0655 from Pyrococcus horikoshii OT3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006566 | biological_process | L-threonine metabolic process |
| A | 0006567 | biological_process | L-threonine catabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008743 | molecular_function | L-threonine 3-dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016597 | molecular_function | amino acid binding |
| A | 0019518 | biological_process | obsolete L-threonine catabolic process to glycine |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0070401 | molecular_function | NADP+ binding |
| A | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | CYS42 |
| A | HIS67 |
| A | GLU68 |
| A | HOH762 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 502 |
| Chain | Residue |
| A | GLU92 |
| A | GLU152 |
| A | HIS295 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 503 |
| Chain | Residue |
| A | HOH634 |
| A | HOH635 |
| A | HOH763 |
| A | HIS94 |
| A | HIS295 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 504 |
| Chain | Residue |
| A | GLU127 |
| A | GLU221 |
| A | HOH764 |
| A | HOH765 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 505 |
| Chain | Residue |
| A | GLU222 |
| A | ASP326 |
| A | HOH766 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD A 401 |
| Chain | Residue |
| A | GLY175 |
| A | GLY177 |
| A | PRO178 |
| A | LEU179 |
| A | SER198 |
| A | GLU199 |
| A | PRO200 |
| A | ARG204 |
| A | PHE243 |
| A | SER244 |
| A | ALA246 |
| A | LEU266 |
| A | GLY267 |
| A | LEU268 |
| A | ILE282 |
| A | ILE291 |
| A | THR292 |
| A | HOH509 |
| A | HOH516 |
| A | HOH580 |
| A | HOH592 |
| A | HOH732 |
| A | HOH747 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEvAGEvveiGpgV |
| Chain | Residue | Details |
| A | GLY66-VAL80 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"18390572","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00627","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2005","submissionDatabase":"PDB data bank","title":"Crystal structure of PH0655 from Pyrococcus horikoshii OT3.","authors":["Asada Y.","Kunishima N."]}},{"source":"PubMed","id":"17188300","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18390572","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2D8A","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00627","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17188300","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2DFV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17188300","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2005","submissionDatabase":"PDB data bank","title":"Crystal structure of PH0655 from Pyrococcus horikoshii OT3.","authors":["Asada Y.","Kunishima N."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17188300","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2005","submissionDatabase":"PDB data bank","title":"Crystal structure of PH0655 from Pyrococcus horikoshii OT3.","authors":["Asada Y.","Kunishima N."]}},{"source":"PDB","id":"2D8A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2DFV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2005","submissionDatabase":"PDB data bank","title":"Crystal structure of PH0655 from Pyrococcus horikoshii OT3.","authors":["Asada Y.","Kunishima N."]}},{"source":"PDB","id":"2D8A","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atom","evidences":[{"source":"PubMed","id":"18390572","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| A | THR44 | |
| A | GLY43 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1teh |
| Chain | Residue | Details |
| A | THR44 | |
| A | HIS47 |
