2CAN
HUMAN ORNITHINE AMINOTRANSFERASE COMPLEXED WITH L-CANALINE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004587 | molecular_function | ornithine aminotransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0007601 | biological_process | visual perception |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0010121 | biological_process | L-arginine catabolic process to proline via ornithine |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019544 | biological_process | L-arginine catabolic process to L-glutamate |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0055129 | biological_process | L-proline biosynthetic process |
| B | 0004587 | molecular_function | ornithine aminotransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0007601 | biological_process | visual perception |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0010121 | biological_process | L-arginine catabolic process to proline via ornithine |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019544 | biological_process | L-arginine catabolic process to L-glutamate |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0055129 | biological_process | L-proline biosynthetic process |
| C | 0004587 | molecular_function | ornithine aminotransferase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005759 | cellular_component | mitochondrial matrix |
| C | 0007601 | biological_process | visual perception |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0010121 | biological_process | L-arginine catabolic process to proline via ornithine |
| C | 0016740 | molecular_function | transferase activity |
| C | 0019544 | biological_process | L-arginine catabolic process to L-glutamate |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0055129 | biological_process | L-proline biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CAN A 1 |
| Chain | Residue |
| A | PLP2 |
| B | THR322 |
| A | TYR55 |
| A | TYR85 |
| A | PHE177 |
| A | ARG180 |
| A | GLU235 |
| A | LYS292 |
| B | GLY320 |
| B | SER321 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP A 2 |
| Chain | Residue |
| A | CAN1 |
| A | GLY142 |
| A | VAL143 |
| A | PHE177 |
| A | TRP178 |
| A | GLU230 |
| A | ASP263 |
| A | ILE265 |
| A | GLN266 |
| A | LYS292 |
| A | HOH476 |
| A | HOH482 |
| B | THR322 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CAN B 1 |
| Chain | Residue |
| A | GLY320 |
| A | SER321 |
| B | PLP2 |
| B | TYR55 |
| B | TYR85 |
| B | PHE177 |
| B | ARG180 |
| B | GLU235 |
| B | LYS292 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 2 |
| Chain | Residue |
| A | THR322 |
| B | CAN1 |
| B | GLY142 |
| B | VAL143 |
| B | PHE177 |
| B | TRP178 |
| B | GLU230 |
| B | ASP263 |
| B | ILE265 |
| B | GLN266 |
| B | LYS292 |
| B | HOH444 |
| B | HOH449 |
| B | HOH482 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CAN C 1 |
| Chain | Residue |
| C | PLP2 |
| C | TYR55 |
| C | TYR85 |
| C | PHE177 |
| C | ARG180 |
| C | GLU235 |
| C | LYS292 |
| C | GLY320 |
| C | SER321 |
| C | THR322 |
| C | HOH502 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP C 2 |
| Chain | Residue |
| C | CAN1 |
| C | GLY142 |
| C | VAL143 |
| C | PHE177 |
| C | TRP178 |
| C | GLU230 |
| C | ASP263 |
| C | ILE265 |
| C | GLN266 |
| C | LYS292 |
| C | THR322 |
| C | HOH442 |
| C | HOH443 |
| C | HOH478 |
| C | HOH482 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FIaDEIqt.GLaRtGrwlavdyenvrp....DIVllGKalsGG |
| Chain | Residue | Details |
| A | PHE260-GLY297 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 15 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P29758","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P29758","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P29758","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"3754226","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP263 | |
| A | TRP178 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP263 | |
| B | TRP178 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | ASP263 | |
| C | TRP178 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LYS292 | |
| A | PHE177 | |
| A | ASP263 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | LYS292 | |
| B | PHE177 | |
| B | ASP263 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | LYS292 | |
| C | PHE177 | |
| C | ASP263 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LYS292 | |
| A | ASP263 | |
| A | TRP178 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | LYS292 | |
| B | ASP263 | |
| B | TRP178 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | LYS292 | |
| C | ASP263 | |
| C | TRP178 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 929 |
| Chain | Residue | Details |
| A | PHE177 | steric role |
| A | ASP263 | electrostatic stabiliser |
| A | LYS292 | covalent catalysis, proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 929 |
| Chain | Residue | Details |
| B | PHE177 | steric role |
| B | ASP263 | electrostatic stabiliser |
| B | LYS292 | covalent catalysis, proton shuttle (general acid/base) |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 929 |
| Chain | Residue | Details |
| C | PHE177 | steric role |
| C | ASP263 | electrostatic stabiliser |
| C | LYS292 | covalent catalysis, proton shuttle (general acid/base) |
