1GPW
Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| A | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| B | 0004359 | molecular_function | glutaminase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009382 | cellular_component | imidazoleglycerol-phosphate synthase complex |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016829 | molecular_function | lyase activity |
| C | 0000105 | biological_process | L-histidine biosynthetic process |
| C | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| D | 0000105 | biological_process | L-histidine biosynthetic process |
| D | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| D | 0004359 | molecular_function | glutaminase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0009382 | cellular_component | imidazoleglycerol-phosphate synthase complex |
| D | 0016763 | molecular_function | pentosyltransferase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016829 | molecular_function | lyase activity |
| E | 0000105 | biological_process | L-histidine biosynthetic process |
| E | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0008652 | biological_process | amino acid biosynthetic process |
| E | 0016829 | molecular_function | lyase activity |
| F | 0000105 | biological_process | L-histidine biosynthetic process |
| F | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| F | 0004359 | molecular_function | glutaminase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0008652 | biological_process | amino acid biosynthetic process |
| F | 0009382 | cellular_component | imidazoleglycerol-phosphate synthase complex |
| F | 0016763 | molecular_function | pentosyltransferase activity |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 301 |
| Chain | Residue |
| A | GLY81 |
| A | GLY82 |
| A | HIS84 |
| A | ASN103 |
| A | THR104 |
| A | HOH425 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 302 |
| Chain | Residue |
| A | ALA223 |
| A | ALA224 |
| A | HOH421 |
| A | ASP176 |
| A | GLY177 |
| A | GLY203 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 C 301 |
| Chain | Residue |
| C | ASP176 |
| C | GLY177 |
| C | GLY203 |
| C | ALA224 |
| C | SER225 |
| C | HOH411 |
| C | HOH452 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 C 302 |
| Chain | Residue |
| C | GLY82 |
| C | ASN103 |
| C | THR104 |
| C | HOH418 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 C 303 |
| Chain | Residue |
| C | LYS37 |
| C | GLN72 |
| C | ASP74 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 E 301 |
| Chain | Residue |
| E | GLY81 |
| E | GLY82 |
| E | THR104 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 597 |
| Details | Domain: {"description":"Glutamine amidotransferase type-1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Active site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| F | GLU180 | |
| F | CYS84 | |
| F | HIS178 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| B | GLU180 | |
| B | CYS84 | |
| B | HIS178 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| D | GLU180 | |
| D | CYS84 | |
| D | HIS178 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| B | CYS84 | |
| B | HIS178 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| F | CYS84 | |
| F | HIS178 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| A | ASN11 | |
| A | ASP130 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| C | ASN11 | |
| C | ASP130 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| E | ASN11 | |
| E | ASP130 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| D | CYS84 | |
| D | HIS178 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 753 |
| Chain | Residue | Details |
| A | ASN11 | proton acceptor, proton donor |
| A | ASP130 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 753 |
| Chain | Residue | Details |
| C | ASN11 | proton acceptor, proton donor |
| C | ASP130 | proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 2 |
| Details | M-CSA 753 |
| Chain | Residue | Details |
| E | ASN11 | proton acceptor, proton donor |
| E | ASP130 | proton acceptor, proton donor |
