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 | 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 | 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
Chain | Residue | Details |
A | LYS212 | |
B | LYS212 | |
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 | |