3PHI
Shikimate 5-Dehydrogenase (aroE) from Helicobacter pylori in complex with Shikimate and NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| A | 0009423 | biological_process | chorismate biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019632 | biological_process | shikimate metabolic process |
| A | 0050661 | molecular_function | NADP binding |
| B | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| B | 0009423 | biological_process | chorismate biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019632 | biological_process | shikimate metabolic process |
| B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SKM A 500 |
| Chain | Residue |
| A | SER16 |
| A | GLN237 |
| A | HOH286 |
| A | NDP1411 |
| A | SER18 |
| A | ASN63 |
| A | VAL64 |
| A | THR65 |
| A | LYS69 |
| A | ASN90 |
| A | ASP105 |
| A | TYR210 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NDP A 1411 |
| Chain | Residue |
| A | LEU66 |
| A | PRO67 |
| A | LYS69 |
| A | ALA126 |
| A | GLY127 |
| A | GLY128 |
| A | SER129 |
| A | ASN148 |
| A | ARG149 |
| A | SER150 |
| A | ALA179 |
| A | THR180 |
| A | SER181 |
| A | LEU184 |
| A | PRO189 |
| A | LEU208 |
| A | TYR210 |
| A | GLY230 |
| A | MET233 |
| A | LEU234 |
| A | HOH273 |
| A | HOH276 |
| A | HOH286 |
| A | HOH306 |
| A | HOH309 |
| A | HOH316 |
| A | HOH347 |
| A | SKM500 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SKM B 500 |
| Chain | Residue |
| B | SER16 |
| B | SER18 |
| B | ASN63 |
| B | THR65 |
| B | LYS69 |
| B | ASN90 |
| B | ASP105 |
| B | TYR210 |
| B | GLN237 |
| B | HOH293 |
| B | NDP1411 |
| site_id | AC4 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NDP B 1411 |
| Chain | Residue |
| B | LEU66 |
| B | PRO67 |
| B | LYS69 |
| B | ASP105 |
| B | GLY125 |
| B | ALA126 |
| B | GLY127 |
| B | GLY128 |
| B | SER129 |
| B | ASN148 |
| B | ARG149 |
| B | SER150 |
| B | ALA179 |
| B | THR180 |
| B | SER181 |
| B | ALA182 |
| B | LEU184 |
| B | GLU187 |
| B | PRO189 |
| B | LEU208 |
| B | TYR210 |
| B | GLY230 |
| B | MET233 |
| B | LEU234 |
| B | HOH271 |
| B | HOH279 |
| B | HOH293 |
| B | HOH297 |
| B | HOH309 |
| B | HOH336 |
| B | HOH339 |
| B | HOH342 |
| B | SKM500 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00222","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of the shikimate 5-dehydrogenase (aroE) from Helicobacter pylori in complex with shikimate and NADPH.","authors":["Cheng W.C.","Lin S.C.","Wang W.C."]}},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"DEC-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of shikimate dehydrogenase (aroE) mutants from Helicobacter pylori in complex with shikimate.","authors":["Cheng W.C.","Lin S.C.","Wang W.C."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00222","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of the shikimate 5-dehydrogenase (aroE) from Helicobacter pylori in complex with shikimate and NADPH.","authors":["Cheng W.C.","Lin S.C.","Wang W.C."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of shikimate dehydrogenase (aroE) mutants from Helicobacter pylori in complex with shikimate.","authors":["Cheng W.C.","Lin S.C.","Wang W.C."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2013","submissionDatabase":"PDB data bank","title":"Crystal structure of shikimate dehydrogenase (aroE) clinical v2356 from Helicobacter pylori in complex with shikimate.","authors":["Cheng W.C.","Chen T.J.","Wang W.C."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00222","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of the shikimate 5-dehydrogenase (aroE) from Helicobacter pylori in complex with shikimate and NADPH.","authors":["Cheng W.C.","Lin S.C.","Wang W.C."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of shikimate dehydrogenase (aroE) mutants from Helicobacter pylori in complex with shikimate.","authors":["Cheng W.C.","Lin S.C.","Wang W.C."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00222","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of the shikimate 5-dehydrogenase (aroE) from Helicobacter pylori in complex with shikimate and NADPH.","authors":["Cheng W.C.","Lin S.C.","Wang W.C."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of the shikimate 5-dehydrogenase (aroE) from Helicobacter pylori in complex with shikimate and NADPH.","authors":["Cheng W.C.","Lin S.C.","Wang W.C."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00222","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00222","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of the shikimate 5-dehydrogenase (aroE) from Helicobacter pylori in complex with shikimate and NADPH.","authors":["Cheng W.C.","Lin S.C.","Wang W.C."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2013","submissionDatabase":"PDB data bank","title":"Crystal structure of shikimate dehydrogenase (aroE) clinical v2356 from Helicobacter pylori in complex with shikimate.","authors":["Cheng W.C.","Chen T.J.","Wang W.C."]}}]} |
| Chain | Residue | Details |
