Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| A | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL A 359 |
| Chain | Residue |
| A | LYS28 |
| A | HOH556 |
| B | ARG58 |
| B | ILE59 |
| A | GLU33 |
| A | ASN34 |
| A | PRO35 |
| A | GLY334 |
| A | GLU338 |
| A | HOH420 |
| A | HOH432 |
| A | HOH469 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 360 |
| Chain | Residue |
| A | GLU348 |
| A | HOH586 |
Functional Information from PROSITE/UniProt
| site_id | PS00599 |
| Number of Residues | 10 |
| Details | AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TLSKSYSLAG |
| Chain | Residue | Details |
| A | THR209-GLY218 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01023","evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LYS212 | |
| A | TYR114 | |
| A | ASP183 | |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ILE59 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | LYS212 | |
| B | TYR114 | |
| B | ASP183 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LYS212 | |
| A | HIS111 | |
| A | ASP183 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | LYS212 | |
| B | HIS111 | |
| B | ASP183 | |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LYS212 | |
| A | TYR117 | |
| A | ASP183 | |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | LYS212 | |
| B | TYR117 | |
| B | ASP183 | |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR114 | |
| A | ASP183 | |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR114 | |
| B | ASP183 | |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ILE59 | |
