4JF0
N79R 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 | 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 | HOH624 |
B | TRP75 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO A 502 |
Chain | Residue |
A | GLY50 |
A | HIS58 |
A | HOH638 |
A | HOH718 |
B | HIS76 |
B | THR77 |
B | SER78 |
B | PHE81 |
B | ACT503 |
A | ASP46 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT A 503 |
Chain | Residue |
A | SER78 |
A | PHE81 |
A | HOH625 |
B | ALA48 |
B | GLY50 |
B | LEU369 |
B | EDO504 |
B | HOH621 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 504 |
Chain | Residue |
A | ILE94 |
A | THR97 |
A | PHE98 |
A | ALA99 |
A | HOH609 |
A | HOH658 |
site_id | AC5 |
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 | HOH608 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 502 |
Chain | Residue |
B | ILE94 |
B | THR97 |
B | PHE98 |
B | ALA99 |
B | HOH601 |
B | HOH606 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT B 503 |
Chain | Residue |
A | ALA48 |
A | GLY50 |
A | LEU369 |
A | EDO502 |
A | HOH638 |
B | SER78 |
B | PHE81 |
B | HOH690 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO B 504 |
Chain | Residue |
A | HIS76 |
A | THR77 |
A | SER78 |
A | PHE81 |
A | ACT503 |
B | ASP46 |
B | GLY50 |
B | HIS58 |
B | HOH621 |
B | HOH706 |
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 | LLP255 | |
B | LLP255 |