4JEZ
N79R mutant of N-acetylornithine aminotransferase 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 | 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 | HOH619 |
| B | TRP75 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT A 502 |
| Chain | Residue |
| A | PHE81 |
| A | EDO503 |
| A | HOH604 |
| A | HOH629 |
| B | ALA48 |
| B | GLY50 |
| B | LEU369 |
| A | SER78 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | HIS76 |
| A | THR77 |
| A | SER78 |
| A | PHE81 |
| A | ACT502 |
| A | HOH604 |
| A | HOH640 |
| B | ASP46 |
| B | GLY50 |
| B | HIS58 |
| B | MET367 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT A 504 |
| Chain | Residue |
| A | TRP37 |
| A | HOH846 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE EDO A 505 |
| Chain | Residue |
| A | ASP46 |
| A | GLY50 |
| A | HIS58 |
| A | MET367 |
| A | HOH663 |
| A | HOH685 |
| B | HIS76 |
| B | THR77 |
| B | SER78 |
| B | PHE81 |
| B | ACT507 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 506 |
| Chain | Residue |
| A | SER128 |
| A | ASP185 |
| A | HIS186 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 507 |
| Chain | Residue |
| A | LYS133 |
| A | ILE168 |
| A | HIS170 |
| A | HOH668 |
| A | HOH684 |
| A | HOH784 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 508 |
| Chain | Residue |
| A | TYR122 |
| A | HIS127 |
| A | GLN220 |
| A | LEU222 |
| A | HOH690 |
| A | HOH835 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA A 509 |
| Chain | Residue |
| A | ILE94 |
| A | THR97 |
| A | PHE98 |
| A | ALA99 |
| A | HOH724 |
| A | HOH745 |
| A | HOH860 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 510 |
| Chain | Residue |
| A | THR205 |
| A | PRO206 |
| A | GLU207 |
| A | HOH737 |
| B | THR205 |
| site_id | BC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE P00 A 511 |
| Chain | Residue |
| A | ILE51 |
| A | SER107 |
| A | GLY108 |
| A | THR109 |
| A | ASN112 |
| A | PHE141 |
| A | HIS142 |
| A | GLU193 |
| A | GLU198 |
| A | ASP226 |
| A | VAL228 |
| A | GLN229 |
| A | LYS255 |
| A | HOH806 |
| B | HOH784 |
| site_id | BC3 |
| 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 | HOH609 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 502 |
| Chain | Residue |
| B | LYS133 |
| B | ILE168 |
| B | HIS170 |
| B | HOH659 |
| B | HOH711 |
| B | HOH724 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 503 |
| Chain | Residue |
| B | SER128 |
| B | ASP185 |
| B | HIS186 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 504 |
| Chain | Residue |
| B | TYR122 |
| B | HIS127 |
| B | GLN220 |
| B | HOH697 |
| site_id | BC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE P00 B 505 |
| Chain | Residue |
| A | HOH744 |
| 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 | HOH745 |
| B | HOH803 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT B 506 |
| Chain | Residue |
| A | VAL80 |
| B | ALA22 |
| B | PRO23 |
| B | PHE26 |
| B | TYR359 |
| B | ALA362 |
| B | HOH650 |
| B | HOH808 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT B 507 |
| Chain | Residue |
| A | ALA48 |
| A | GLY50 |
| A | LEU369 |
| A | EDO505 |
| A | HOH685 |
| B | SER78 |
| B | PHE81 |
| B | HOH676 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 508 |
| Chain | Residue |
| B | ILE94 |
| B | THR97 |
| B | PHE98 |
| B | ALA99 |
| B | HOH736 |
| B | HOH771 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 509 |
| Chain | Residue |
| A | THR205 |
| A | HOH864 |
| B | THR205 |
| B | PRO206 |
| B | GLU207 |
| B | HOH791 |
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 |
