4JEV
N-acetylornithine aminotransferase from S. typhimurium complexed with gabaculine
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 | arginine biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009016 | molecular_function | succinyldiaminopimelate transaminase activity |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| 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 | arginine biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009016 | molecular_function | succinyldiaminopimelate transaminase activity |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PXG A 501 |
| Chain | Residue |
| A | ILE51 |
| A | ASP226 |
| A | VAL228 |
| A | GLN229 |
| A | LYS255 |
| A | ARG377 |
| A | HOH677 |
| A | HOH727 |
| A | HOH754 |
| B | THR284 |
| B | HOH691 |
| A | SER107 |
| A | GLY108 |
| A | THR109 |
| A | ASN112 |
| A | PHE141 |
| A | HIS142 |
| A | GLU193 |
| A | GLU198 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT A 502 |
| Chain | Residue |
| A | LYS133 |
| A | ILE168 |
| A | ILE169 |
| A | HIS170 |
| A | HOH656 |
| A | HOH713 |
| A | HOH851 |
| A | HOH927 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA A 503 |
| Chain | Residue |
| A | ILE94 |
| A | THR97 |
| A | PHE98 |
| A | ALA99 |
| A | HOH794 |
| A | HOH837 |
| A | HOH951 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE PXG B 501 |
| Chain | Residue |
| A | THR284 |
| A | HOH649 |
| B | ILE51 |
| B | SER107 |
| B | GLY108 |
| B | THR109 |
| B | ASN112 |
| B | PHE141 |
| B | HIS142 |
| B | GLU193 |
| B | GLU198 |
| B | ASP226 |
| B | VAL228 |
| B | GLN229 |
| B | LYS255 |
| B | ARG377 |
| B | HOH659 |
| B | HOH677 |
| B | HOH685 |
| B | HOH959 |
| B | HOH960 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT B 502 |
| Chain | Residue |
| B | LYS133 |
| B | ILE168 |
| B | HIS170 |
| B | HOH657 |
| B | HOH670 |
| B | HOH755 |
| B | HOH933 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 503 |
| Chain | Residue |
| B | ILE94 |
| B | THR97 |
| B | PHE98 |
| B | ALA99 |
| B | HOH603 |
| B | HOH931 |
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: BINDING => ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|PubMed:17680699 |
| Chain | Residue | Details |
| A | GLY108 | |
| A | THR284 | |
| B | GLY108 | |
| B | THR284 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000305|PubMed:17680699 |
| Chain | Residue | Details |
| A | PHE141 | |
| A | ASP226 | |
| B | PHE141 | |
| B | ASP226 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107 |
| Chain | Residue | Details |
| A | ARG144 | |
| A | SER283 | |
| B | ARG144 | |
| B | SER283 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|PubMed:17680699 |
| Chain | Residue | Details |
| A | LYS255 | |
| B | LYS255 |
