Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000105 | biological_process | L-histidine biosynthetic process |
A | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue MN A 401 |
Chain | Residue |
A | HIS47 |
A | HIS74 |
A | HIS169 |
A | GLU173 |
A | 5DL403 |
A | 5LD404 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue MN A 402 |
Chain | Residue |
A | HIS170 |
A | 5DL403 |
A | 5LD404 |
A | HOH525 |
A | HIS73 |
A | GLU77 |
A | HIS145 |
site_id | AC3 |
Number of Residues | 21 |
Details | binding site for residue 5DL A 403 |
Chain | Residue |
A | GLU21 |
A | HIS47 |
A | HIS73 |
A | HIS74 |
A | GLU77 |
A | ARG99 |
A | LEU107 |
A | ARG121 |
A | HIS169 |
A | HIS170 |
A | GLU173 |
A | LYS177 |
A | SER199 |
A | LYS201 |
A | MN401 |
A | MN402 |
A | 5LD404 |
A | EDO409 |
A | HOH525 |
A | HOH574 |
A | HOH607 |
site_id | AC4 |
Number of Residues | 20 |
Details | binding site for residue 5LD A 404 |
Chain | Residue |
A | GLU21 |
A | HIS47 |
A | HIS73 |
A | HIS74 |
A | GLU77 |
A | ARG99 |
A | ARG121 |
A | HIS169 |
A | HIS170 |
A | GLU173 |
A | LYS177 |
A | SER199 |
A | LYS201 |
A | MN401 |
A | MN402 |
A | 5DL403 |
A | EDO409 |
A | HOH525 |
A | HOH574 |
A | HOH607 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue EDO A 405 |
Chain | Residue |
A | LEU88 |
A | ARG94 |
A | LEU118 |
A | SER119 |
A | GLY120 |
A | SER154 |
A | GLY155 |
A | HOH532 |
A | HOH580 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO A 406 |
Chain | Residue |
A | ARG17 |
A | THR85 |
A | THR153 |
A | HOH537 |
A | HOH545 |
A | HOH697 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue EDO A 407 |
Chain | Residue |
A | GLN133 |
A | GLN133 |
A | GLN133 |
A | GLN133 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue EDO A 408 |
Chain | Residue |
A | ASN23 |
A | ASN23 |
A | SER25 |
A | ARG63 |
A | HOH501 |
A | HOH511 |
A | HOH577 |
A | HOH695 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue EDO A 409 |
Chain | Residue |
A | GLU21 |
A | GLU77 |
A | ASP78 |
A | LYS201 |
A | 5DL403 |
A | 5LD404 |
A | HOH504 |
A | HOH652 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue EDO A 410 |
Chain | Residue |
A | SER36 |
A | ASP37 |
A | SER38 |
A | ASP50 |
A | HOH505 |
site_id | AD2 |
Number of Residues | 14 |
Details | binding site for residue TRS A 411 |
Chain | Residue |
A | HIS113 |
A | ARG161 |
A | ARG161 |
A | ARG161 |
A | LEU163 |
A | LEU163 |
A | HOH520 |
A | HOH520 |
A | HOH520 |
A | THR104 |
A | THR104 |
A | THR104 |
A | HIS113 |
A | HIS113 |
site_id | AD3 |
Number of Residues | 12 |
Details | binding site for residue TRS A 412 |
Chain | Residue |
A | ASP102 |
A | ASP102 |
A | ASP102 |
A | PHE103 |
A | PHE103 |
A | PHE103 |
A | GLN185 |
A | GLN185 |
A | GLN185 |
A | HOH619 |
A | HOH619 |
A | HOH619 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue CL A 413 |
Chain | Residue |
A | ARG161 |
A | ARG161 |
A | ARG161 |
Functional Information from PROSITE/UniProt
site_id | PS00954 |
Number of Residues | 14 |
Details | IGP_DEHYDRATASE_1 Imidazoleglycerol-phosphate dehydratase signature 1. IDdHHtnEdvALAI |
Chain | Residue | Details |
A | ILE70-ILE83 | |
site_id | PS00955 |
Number of Residues | 13 |
Details | IGP_DEHYDRATASE_2 Imidazoleglycerol-phosphate dehydratase signature 2. GkNsHHiiEAtFK |
Chain | Residue | Details |
A | GLY165-LYS177 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU21 | |
Chain | Residue | Details |
A | HIS47 | |
A | HIS74 | |
A | HIS169 | |
A | GLU173 | |
Chain | Residue | Details |
A | HIS73 | |
A | GLU77 | |
A | HIS145 | |
A | HIS170 | |
Chain | Residue | Details |
A | ARG99 | |
Chain | Residue | Details |
A | ARG121 | |
A | SER199 | |