3ZR4
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 | 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 | 0006541 | biological_process | glutamine metabolic process |
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 | 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 | 0006541 | biological_process | glutamine metabolic process |
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 | 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 | 0006541 | biological_process | glutamine metabolic process |
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 | 1 |
Details | BINDING SITE FOR RESIDUE GOL A 1202 |
Chain | Residue |
A | GLU231 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 1201 |
Chain | Residue |
B | PRO38 |
B | ARG39 |
B | ASN40 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GLN B 1205 |
Chain | Residue |
B | GLU96 |
B | VAL140 |
B | HIS141 |
B | THR142 |
B | TYR143 |
B | HOH2030 |
B | HOH2036 |
A | GLN123 |
B | VAL51 |
B | GLY52 |
B | CYS84 |
B | GLN88 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE GOL B 1202 |
Chain | Residue |
B | LYS72 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 1254 |
Chain | Residue |
C | ASN148 |
C | THR149 |
C | GLY150 |
C | HOH2035 |
D | ASN26 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL D 1201 |
Chain | Residue |
D | LYS129 |
D | ASP130 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GLN D 1205 |
Chain | Residue |
D | GLY52 |
D | GLN88 |
D | GLU96 |
D | VAL140 |
D | HIS141 |
D | THR142 |
D | TYR143 |
D | HOH2029 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL E 1254 |
Chain | Residue |
E | ARG188 |
E | LEU215 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL E 1255 |
Chain | Residue |
D | GLU36 |
E | ARG188 |
E | PHE189 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
B | CYS84 | |
D | CYS84 | |
F | CYS84 | |
C | ASP130 | |
E | ASP11 | |
E | ASP130 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | ACT_SITE: |
Chain | Residue | Details |
B | HIS178 | |
B | GLU180 | |
D | HIS178 | |
D | GLU180 | |
F | HIS178 | |
F | GLU180 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 753 |
Chain | Residue | Details |
A | ASP11 | 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 | ASP11 | 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 | ASP11 | proton acceptor, proton donor |
E | ASP130 | proton acceptor, proton donor |