1CI0
PNP OXIDASE FROM SACCHAROMYCES CEREVISIAE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004733 | molecular_function | pyridoxamine phosphate oxidase activity |
| A | 0005758 | cellular_component | mitochondrial intermembrane space |
| A | 0008615 | biological_process | pyridoxine biosynthetic process |
| A | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| A | 0042816 | biological_process | vitamin B6 metabolic process |
| B | 0004733 | molecular_function | pyridoxamine phosphate oxidase activity |
| B | 0005758 | cellular_component | mitochondrial intermembrane space |
| B | 0008615 | biological_process | pyridoxine biosynthetic process |
| B | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| B | 0042816 | biological_process | vitamin B6 metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE FMN B 300 |
| Chain | Residue |
| A | PHE111 |
| B | SER89 |
| B | SER94 |
| B | ARG95 |
| B | LYS96 |
| B | GLN153 |
| B | SER154 |
| A | GLN118 |
| A | ARG120 |
| A | TRP199 |
| A | ARG209 |
| B | ARG73 |
| B | ILE74 |
| B | LEU75 |
| B | TYR88 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE FMN A 301 |
| Chain | Residue |
| A | ARG73 |
| A | ILE74 |
| A | LEU75 |
| A | TYR88 |
| A | SER89 |
| A | SER94 |
| A | ARG95 |
| A | LYS96 |
| A | GLN153 |
| A | SER154 |
| B | PHE111 |
| B | GLN118 |
| B | ARG120 |
| B | TRP199 |
| B | ARG209 |
Functional Information from PROSITE/UniProt
| site_id | PS01064 |
| Number of Residues | 14 |
| Details | PYRIDOX_OXIDASE Pyridoxamine 5'-phosphate oxidase signature. IEFWQgrpsRLHDR |
| Chain | Residue | Details |
| A | ILE196-ARG209 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2005","submissionDatabase":"PDB data bank","title":"The structure of PNP oxidase from S. cerevisiae.","authoringGroup":["New York structural genomix research consortium (NYSGXRC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9NVS9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0AFI7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"12872131","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1g79 |
| Chain | Residue | Details |
| A | ARG205 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1g79 |
| Chain | Residue | Details |
| B | ARG205 |
