2PB0
Structure of biosynthetic N-acetylornithine aminotransferase from Salmonella typhimurium: studies on substrate specificity and inhibitor binding
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 | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 555 |
| Chain | Residue |
| A | SER107 |
| A | GLN229 |
| A | LYS255 |
| A | HOH1154 |
| A | HOH1225 |
| A | HOH1226 |
| B | THR284 |
| B | HOH1108 |
| A | GLY108 |
| A | THR109 |
| A | ASN112 |
| A | PHE141 |
| A | HIS142 |
| A | GLU193 |
| A | ASP226 |
| A | VAL228 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP B 555 |
| Chain | Residue |
| B | SER107 |
| B | GLY108 |
| B | THR109 |
| B | ASN112 |
| B | PHE141 |
| B | HIS142 |
| B | GLU193 |
| B | ASP226 |
| B | VAL228 |
| B | GLN229 |
| B | LYS255 |
| B | HOH1142 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 1001 |
| Chain | Residue |
| A | TRP75 |
| B | GLY57 |
| B | HIS58 |
| B | CYS59 |
| B | HIS60 |
| B | GLY259 |
| B | HOH1031 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 1002 |
| Chain | Residue |
| A | GLY57 |
| A | HIS58 |
| A | CYS59 |
| A | HIS60 |
| A | GLY259 |
| A | HOH1037 |
| B | TRP75 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B 1003 |
| Chain | Residue |
| A | THR109 |
| A | ARG144 |
| A | SER145 |
| B | MET105 |
| B | GLU110 |
| B | GLU113 |
| B | THR114 |
| B | HIS281 |
| B | HOH1147 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1004 |
| Chain | Residue |
| A | PRO206 |
| A | HOH1260 |
| A | HOH1261 |
| A | HOH1266 |
| B | PRO206 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP226 | |
| A | PHE141 | |
| A | LYS255 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP226 | |
| B | PHE141 | |
| B | LYS255 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP226 | |
| A | PHE141 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP226 | |
| B | PHE141 |
