4JEW
N-acetylornithine aminotransferase from S. typhimurium complexed with L-canaline
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 | L-lysine biosynthetic process |
| A | 0009089 | biological_process | L-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 |
| 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 | L-lysine biosynthetic process |
| B | 0009089 | biological_process | L-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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE P00 A 501 |
| Chain | Residue |
| A | SER107 |
| A | GLU198 |
| A | ASP226 |
| A | VAL228 |
| A | GLN229 |
| A | LYS255 |
| A | HOH636 |
| A | HOH666 |
| A | HOH697 |
| A | HOH700 |
| A | HOH708 |
| A | GLY108 |
| B | GLY282 |
| B | SER283 |
| B | THR284 |
| B | HOH633 |
| A | THR109 |
| A | ASN112 |
| A | PHE141 |
| A | HIS142 |
| A | GLY143 |
| A | ARG144 |
| A | GLU193 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT A 502 |
| Chain | Residue |
| A | SER78 |
| A | VAL80 |
| A | PHE81 |
| A | EDO504 |
| A | HOH620 |
| A | HOH677 |
| B | ALA48 |
| B | GLY50 |
| B | LEU369 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | GLY57 |
| A | HIS58 |
| A | CYS59 |
| A | HIS60 |
| A | LEU63 |
| A | GLY259 |
| A | HOH605 |
| B | TRP75 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE EDO A 504 |
| Chain | Residue |
| A | HIS76 |
| A | THR77 |
| A | SER78 |
| A | PHE81 |
| A | ACT502 |
| A | HOH620 |
| A | HOH833 |
| B | ASP46 |
| B | GLY50 |
| B | HIS58 |
| B | MET367 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 505 |
| Chain | Residue |
| A | TYR122 |
| A | GLU271 |
| A | HOH651 |
| A | HOH687 |
| A | HOH757 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 506 |
| Chain | Residue |
| A | SER128 |
| A | LYS131 |
| A | ASP185 |
| A | HIS186 |
| A | HOH879 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TNF A 507 |
| Chain | Residue |
| A | LYS30 |
| A | LYS32 |
| A | TRP37 |
| A | GLY41 |
| B | LEU18 |
| B | PRO19 |
| B | TYR21 |
| B | ARG355 |
| B | TYR359 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 508 |
| Chain | Residue |
| A | LYS133 |
| A | ILE168 |
| A | HIS170 |
| A | HOH616 |
| A | HOH675 |
| A | HOH680 |
| A | HOH707 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 509 |
| Chain | Residue |
| A | THR6 |
| A | ILE8 |
| A | HOH844 |
| B | ARG88 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT B 501 |
| Chain | Residue |
| A | VAL80 |
| B | ALA22 |
| B | PRO23 |
| B | PHE26 |
| B | TYR359 |
| B | ALA362 |
| B | HOH676 |
| B | HOH813 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 502 |
| Chain | Residue |
| A | TRP75 |
| B | GLY57 |
| B | HIS58 |
| B | CYS59 |
| B | HIS60 |
| B | LEU63 |
| B | GLY259 |
| B | HOH640 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 503 |
| Chain | Residue |
| B | ILE272 |
| B | HOH698 |
| B | HOH727 |
| B | TYR122 |
| B | GLU271 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 504 |
| Chain | Residue |
| A | PHE13 |
| B | ASN79 |
| B | THR82 |
| B | ASN83 |
| B | ALA86 |
| B | GLY287 |
| B | HOH638 |
| B | HOH710 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT B 505 |
| Chain | Residue |
| B | LYS133 |
| B | ILE168 |
| B | HIS170 |
| B | HOH693 |
| B | HOH695 |
| B | HOH744 |
| B | HOH862 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 506 |
| Chain | Residue |
| A | VAL80 |
| B | LEU369 |
| B | ASN370 |
| B | ARG377 |
| B | HOH907 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 507 |
| Chain | Residue |
| B | SER128 |
| B | ASP185 |
| B | HIS186 |
| site_id | BC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE P00 B 508 |
| Chain | Residue |
| A | HOH782 |
| 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 | HOH721 |
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 |
