4JF1
R144Q 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 | 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 | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 501 |
| Chain | Residue |
| A | SER107 |
| A | GLN229 |
| A | LYS255 |
| A | HOH795 |
| A | HOH867 |
| A | HOH948 |
| B | THR284 |
| B | HOH705 |
| A | GLY108 |
| A | THR109 |
| A | ASN112 |
| A | PHE141 |
| A | HIS142 |
| A | GLU193 |
| A | ASP226 |
| A | VAL228 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 502 |
| Chain | Residue |
| A | GLY57 |
| A | HIS58 |
| A | CYS59 |
| A | HIS60 |
| A | LEU63 |
| A | GLY259 |
| A | HOH618 |
| B | TRP75 |
| 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 | ACT504 |
| A | HOH658 |
| A | HOH660 |
| B | ASP46 |
| B | GLY50 |
| B | HIS58 |
| B | MET367 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACT A 504 |
| Chain | Residue |
| A | SER78 |
| A | VAL80 |
| A | PHE81 |
| A | EDO503 |
| A | HOH658 |
| A | HOH686 |
| B | ALA48 |
| B | GLY50 |
| B | MET367 |
| B | LEU369 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 505 |
| Chain | Residue |
| A | ASP326 |
| A | PHE332 |
| A | HOH715 |
| B | HOH743 |
| B | HOH845 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT A 506 |
| Chain | Residue |
| A | LYS133 |
| A | ILE168 |
| A | HIS170 |
| A | HOH642 |
| A | HOH667 |
| A | HOH727 |
| A | HOH797 |
| A | HOH961 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP B 501 |
| Chain | Residue |
| A | HOH759 |
| B | SER107 |
| B | GLY108 |
| B | THR109 |
| B | ASN112 |
| B | PHE141 |
| B | HIS142 |
| B | GLU193 |
| B | ASP226 |
| B | VAL228 |
| B | GLN229 |
| B | LYS255 |
| B | HOH935 |
| site_id | AC8 |
| 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 | HOH626 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACT B 503 |
| Chain | Residue |
| A | ALA48 |
| A | GLY50 |
| A | LEU369 |
| B | THR77 |
| B | SER78 |
| B | VAL80 |
| B | PHE81 |
| B | EDO504 |
| B | HOH685 |
| B | HOH740 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO B 504 |
| Chain | Residue |
| A | ASP46 |
| A | GLY50 |
| A | HIS58 |
| B | HIS76 |
| B | THR77 |
| B | SER78 |
| B | PHE81 |
| B | ACT503 |
| B | HOH645 |
| B | HOH740 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT B 505 |
| Chain | Residue |
| B | LYS133 |
| B | ILE168 |
| B | HIS170 |
| B | HOH665 |
| B | HOH694 |
| B | HOH713 |
| B | HOH805 |
| B | HOH932 |
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 | GLN144 | |
| A | SER283 | |
| B | GLN144 | |
| 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 |
