2AE8
Crystal Structure of Imidazoleglycerol-phosphate Dehydratase from Staphylococcus aureus subsp. aureus N315
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 |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000105 | biological_process | L-histidine biosynthetic process |
| C | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016829 | molecular_function | lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000105 | biological_process | L-histidine biosynthetic process |
| D | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016829 | molecular_function | lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000105 | biological_process | L-histidine biosynthetic process |
| E | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0016829 | molecular_function | lyase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000105 | biological_process | L-histidine biosynthetic process |
| F | 0004424 | molecular_function | imidazoleglycerol-phosphate dehydratase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0016829 | molecular_function | lyase activity |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1001 |
| Chain | Residue |
| A | HIS36 |
| A | HIS63 |
| A | HIS158 |
| A | GLU162 |
| A | MG1003 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1002 |
| Chain | Residue |
| A | HOH1156 |
| A | HOH1163 |
| A | HIS62 |
| A | GLU66 |
| A | HIS159 |
| A | HOH1046 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1003 |
| Chain | Residue |
| A | MSE96 |
| A | GLU162 |
| A | MG1001 |
| A | HOH1157 |
| A | HOH1163 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1004 |
| Chain | Residue |
| B | HIS62 |
| B | GLU66 |
| B | HOH1018 |
| B | HOH1154 |
| B | HOH1160 |
| C | HIS159 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 1005 |
| Chain | Residue |
| B | HIS159 |
| F | HIS62 |
| F | GLU66 |
| F | HOH1092 |
| F | HOH1153 |
| F | HOH1158 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1006 |
| Chain | Residue |
| A | ARG137 |
| A | ILE141 |
| A | HOH1081 |
| B | PRO111 |
| B | ILE141 |
| B | HOH1008 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1007 |
| Chain | Residue |
| B | HIS36 |
| B | HIS158 |
| B | GLU162 |
| B | HOH1159 |
| F | HIS63 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 1008 |
| Chain | Residue |
| B | HIS63 |
| C | HIS36 |
| C | HIS158 |
| C | GLU162 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 1009 |
| Chain | Residue |
| C | HIS62 |
| C | GLU66 |
| C | HOH1036 |
| C | HOH1155 |
| C | HOH1164 |
| D | HIS159 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 1010 |
| Chain | Residue |
| C | HIS63 |
| D | HIS36 |
| D | HIS158 |
| D | GLU162 |
| D | HOH1148 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 1011 |
| Chain | Residue |
| B | HIS62 |
| B | GLU130 |
| B | LEU131 |
| B | HOH1044 |
| C | ASN156 |
| C | HIS158 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 1012 |
| Chain | Residue |
| D | HIS62 |
| D | GLU66 |
| D | HOH1142 |
| F | HIS159 |
| F | HOH1055 |
| F | HOH1073 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG E 1013 |
| Chain | Residue |
| E | HIS36 |
| E | HIS63 |
| E | HIS158 |
| E | GLU162 |
| E | HOH1203 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 1014 |
| Chain | Residue |
| E | HIS62 |
| E | GLU66 |
| E | HIS159 |
| E | HOH1200 |
| E | HOH1201 |
| E | HOH1202 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 1015 |
| Chain | Residue |
| E | GLU98 |
| E | GLU134 |
| E | ARG137 |
| E | HOH1095 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG F 1016 |
| Chain | Residue |
| D | HIS63 |
| F | HIS36 |
| F | HIS158 |
| F | GLU162 |
Functional Information from PROSITE/UniProt
| site_id | PS00954 |
| Number of Residues | 14 |
| Details | IGP_DEHYDRATASE_1 Imidazoleglycerol-phosphate dehydratase signature 1. VDdHHvtEdiGIVI |
| Chain | Residue | Details |
| A | VAL59-ILE72 |
| site_id | PS00955 |
| Number of Residues | 13 |
| Details | IGP_DEHYDRATASE_2 Imidazoleglycerol-phosphate dehydratase signature 2. GgNtHHeiEAiFK |
| Chain | Residue | Details |
| A | GLY154-LYS166 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O23346 |
| Chain | Residue | Details |
| A | GLU11 | |
| C | ARG88 | |
| C | ARG110 | |
| C | SER186 | |
| D | GLU11 | |
| D | ARG88 | |
| D | ARG110 | |
| D | SER186 | |
| E | GLU11 | |
| E | ARG88 | |
| E | ARG110 | |
| A | ARG88 | |
| E | SER186 | |
| F | GLU11 | |
| F | ARG88 | |
| F | ARG110 | |
| F | SER186 | |
| A | ARG110 | |
| A | SER186 | |
| B | GLU11 | |
| B | ARG88 | |
| B | ARG110 | |
| B | SER186 | |
| C | GLU11 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 48 |
| Details | BINDING: BINDING => ECO:0000305|Ref.2, ECO:0007744|PDB:2AE8 |
| Chain | Residue | Details |
| A | HIS36 | |
| B | HIS62 | |
| B | HIS63 | |
| B | GLU66 | |
| B | GLU134 | |
| B | HIS158 | |
| B | HIS159 | |
| B | GLU162 | |
| C | HIS36 | |
| C | HIS62 | |
| C | HIS63 | |
| A | HIS62 | |
| C | GLU66 | |
| C | GLU134 | |
| C | HIS158 | |
| C | HIS159 | |
| C | GLU162 | |
| D | HIS36 | |
| D | HIS62 | |
| D | HIS63 | |
| D | GLU66 | |
| D | GLU134 | |
| A | HIS63 | |
| D | HIS158 | |
| D | HIS159 | |
| D | GLU162 | |
| E | HIS36 | |
| E | HIS62 | |
| E | HIS63 | |
| E | GLU66 | |
| E | GLU134 | |
| E | HIS158 | |
| E | HIS159 | |
| A | GLU66 | |
| E | GLU162 | |
| F | HIS36 | |
| F | HIS62 | |
| F | HIS63 | |
| F | GLU66 | |
| F | GLU134 | |
| F | HIS158 | |
| F | HIS159 | |
| F | GLU162 | |
| A | GLU134 | |
| A | HIS158 | |
| A | HIS159 | |
| A | GLU162 | |
| B | HIS36 |
