1WKH
Acetylornithine aminotransferase from thermus thermophilus HB8
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006525 | biological_process | arginine metabolic process |
| A | 0006526 | biological_process | arginine biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0006526 | biological_process | arginine biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE PPE A 513 |
| Chain | Residue |
| A | TYR54 |
| A | ILE227 |
| A | GLN228 |
| A | LYS254 |
| A | ARG371 |
| A | HOH515 |
| A | HOH518 |
| A | HOH521 |
| A | HOH526 |
| A | HOH560 |
| B | THR283 |
| A | SER112 |
| B | HOH1517 |
| A | GLY113 |
| A | THR114 |
| A | PHE140 |
| A | SER141 |
| A | GLU192 |
| A | GLU197 |
| A | ASP225 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PPE B 1513 |
| Chain | Residue |
| A | THR283 |
| A | HOH549 |
| B | SER112 |
| B | GLY113 |
| B | THR114 |
| B | PHE140 |
| B | SER141 |
| B | GLU192 |
| B | GLU197 |
| B | ASP225 |
| B | ILE227 |
| B | GLN228 |
| B | LYS254 |
| B | ARG371 |
| B | HOH1514 |
| B | HOH1519 |
| B | HOH1525 |
| B | HOH1528 |
| B | HOH1624 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIlDEIqt.GMgRtGkrfafehfgivp....DILtlAKalgGG |
| Chain | Residue | Details |
| A | LEU222-GLY259 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02084, ECO:0000269|Ref.2 |
| Chain | Residue | Details |
| A | GLY113 | |
| A | THR283 | |
| B | GLY113 | |
| B | THR283 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02084, ECO:0000305|Ref.2 |
| Chain | Residue | Details |
| A | PHE140 | |
| A | ARG143 | |
| A | ASP225 | |
| A | THR282 | |
| B | PHE140 | |
| B | ARG143 | |
| B | ASP225 | |
| B | THR282 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_02084, ECO:0000269|Ref.2 |
| Chain | Residue | Details |
| A | LYS254 | |
| B | LYS254 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LYS254 | |
| A | PHE140 | |
| A | ASP225 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | LYS254 | |
| B | PHE140 | |
| B | ASP225 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | THR95 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | THR95 |
