4JF0
N79R mutant of N-acetylornithine aminotransferase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006525 | biological_process | arginine metabolic process |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009016 | molecular_function | succinyldiaminopimelate transaminase activity |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043648 | biological_process | dicarboxylic acid metabolic process |
| B | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009016 | molecular_function | succinyldiaminopimelate transaminase activity |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043648 | biological_process | dicarboxylic acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 501 |
| Chain | Residue |
| A | GLY57 |
| A | HIS58 |
| A | CYS59 |
| A | HIS60 |
| A | LEU63 |
| A | GLY259 |
| A | HOH624 |
| B | TRP75 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO A 502 |
| Chain | Residue |
| A | GLY50 |
| A | HIS58 |
| A | HOH638 |
| A | HOH718 |
| B | HIS76 |
| B | THR77 |
| B | SER78 |
| B | PHE81 |
| B | ACT503 |
| A | ASP46 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT A 503 |
| Chain | Residue |
| A | SER78 |
| A | PHE81 |
| A | HOH625 |
| B | ALA48 |
| B | GLY50 |
| B | LEU369 |
| B | EDO504 |
| B | HOH621 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 504 |
| Chain | Residue |
| A | ILE94 |
| A | THR97 |
| A | PHE98 |
| A | ALA99 |
| A | HOH609 |
| A | HOH658 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 501 |
| Chain | Residue |
| A | TRP75 |
| B | GLY57 |
| B | HIS58 |
| B | CYS59 |
| B | HIS60 |
| B | LEU63 |
| B | GLY259 |
| B | HOH608 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 502 |
| Chain | Residue |
| B | ILE94 |
| B | THR97 |
| B | PHE98 |
| B | ALA99 |
| B | HOH601 |
| B | HOH606 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT B 503 |
| Chain | Residue |
| A | ALA48 |
| A | GLY50 |
| A | LEU369 |
| A | EDO502 |
| A | HOH638 |
| B | SER78 |
| B | PHE81 |
| B | HOH690 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO B 504 |
| Chain | Residue |
| A | HIS76 |
| A | THR77 |
| A | SER78 |
| A | PHE81 |
| A | ACT503 |
| B | ASP46 |
| B | GLY50 |
| B | HIS58 |
| B | HOH621 |
| B | HOH706 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LVfDEVqc.GMgRtGdlfaymhygvtp....DILtsAKalgGG |
| Chain | Residue | Details |
| A | LEU223-GLY260 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17680699","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17680699","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17680699","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
