1WUR
Structure of GTP cyclohydrolase I Complexed with 8-oxo-dGTP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003934 | molecular_function | GTP cyclohydrolase I activity |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003934 | molecular_function | GTP cyclohydrolase I activity |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003934 | molecular_function | GTP cyclohydrolase I activity |
| C | 0005525 | molecular_function | GTP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| C | 0006730 | biological_process | one-carbon metabolic process |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003934 | molecular_function | GTP cyclohydrolase I activity |
| D | 0005525 | molecular_function | GTP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| D | 0006730 | biological_process | one-carbon metabolic process |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0003934 | molecular_function | GTP cyclohydrolase I activity |
| E | 0005525 | molecular_function | GTP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| E | 0006730 | biological_process | one-carbon metabolic process |
| E | 0008270 | molecular_function | zinc ion binding |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| E | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| A | CYS108 |
| A | HIS111 |
| A | CYS179 |
| A | 8DG821 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1002 |
| Chain | Residue |
| B | CYS108 |
| B | HIS111 |
| B | CYS179 |
| C | 8DG822 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 1003 |
| Chain | Residue |
| C | HIS111 |
| C | CYS179 |
| D | 8DG823 |
| C | CYS108 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 1004 |
| Chain | Residue |
| D | CYS108 |
| D | HIS111 |
| D | CYS179 |
| D | 8DG824 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 1005 |
| Chain | Residue |
| A | 8DG825 |
| E | CYS108 |
| E | HIS111 |
| E | CYS179 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE 8DG A 821 |
| Chain | Residue |
| A | CYS108 |
| A | HIS110 |
| A | HIS111 |
| A | VAL148 |
| A | GLN149 |
| A | GLU150 |
| A | HIS177 |
| A | CYS179 |
| A | ARG183 |
| A | ZN1001 |
| A | HOH1012 |
| A | HOH1038 |
| A | HOH1060 |
| A | HOH1079 |
| B | ALA87 |
| B | LEU130 |
| B | GLY131 |
| B | LEU132 |
| B | SER133 |
| B | LYS134 |
| B | ARG137 |
| E | ARG64 |
| E | HOH1029 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE 8DG C 822 |
| Chain | Residue |
| B | CYS108 |
| B | HIS110 |
| B | HIS111 |
| B | VAL148 |
| B | GLN149 |
| B | GLU150 |
| B | HIS177 |
| B | CYS179 |
| B | ARG183 |
| B | ZN1002 |
| B | HOH1010 |
| C | ALA87 |
| C | LEU130 |
| C | GLY131 |
| C | LEU132 |
| C | SER133 |
| C | LYS134 |
| C | ARG137 |
| D | ARG64 |
| D | HOH1043 |
| site_id | AC8 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 8DG D 823 |
| Chain | Residue |
| C | ARG64 |
| C | CYS108 |
| C | HIS110 |
| C | HIS111 |
| C | VAL148 |
| C | GLN149 |
| C | GLU150 |
| C | HIS177 |
| C | CYS179 |
| C | ARG183 |
| C | ZN1003 |
| C | HOH1019 |
| C | HOH1046 |
| D | ALA87 |
| D | LEU130 |
| D | GLY131 |
| D | LEU132 |
| D | SER133 |
| D | LYS134 |
| D | ARG137 |
| D | HOH1008 |
| D | HOH1050 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 8DG D 824 |
| Chain | Residue |
| E | ALA87 |
| E | LEU130 |
| E | GLY131 |
| E | LEU132 |
| E | SER133 |
| E | LYS134 |
| E | ARG137 |
| B | ARG64 |
| B | HOH1042 |
| D | CYS108 |
| D | HIS110 |
| D | HIS111 |
| D | VAL148 |
| D | GLN149 |
| D | GLU150 |
| D | HIS177 |
| D | CYS179 |
| D | ARG183 |
| D | ZN1004 |
| D | HOH1005 |
| D | HOH1052 |
| site_id | BC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE 8DG A 825 |
| Chain | Residue |
| A | ARG64 |
| A | ALA87 |
| A | LEU130 |
| A | GLY131 |
| A | LEU132 |
| A | SER133 |
| A | LYS134 |
| A | ARG137 |
| A | HOH1039 |
| A | HOH1042 |
| E | CYS108 |
| E | HIS110 |
| E | HIS111 |
| E | VAL148 |
| E | GLN149 |
| E | GLU150 |
| E | HIS177 |
| E | CYS179 |
| E | ARG183 |
| E | ZN1005 |
| E | HOH1022 |
| E | HOH1023 |
Functional Information from PROSITE/UniProt
| site_id | PS00859 |
| Number of Residues | 17 |
| Details | GTP_CYCLOHYDROL_1_1 GTP cyclohydrolase I signature 1. EMVvvKGVefySmCEHH |
| Chain | Residue | Details |
| A | GLU95-HIS111 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1gtp |
| Chain | Residue | Details |
| A | HIS177 | |
| A | HIS110 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1gtp |
| Chain | Residue | Details |
| B | HIS177 | |
| B | HIS110 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1gtp |
| Chain | Residue | Details |
| C | HIS177 | |
| C | HIS110 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1gtp |
| Chain | Residue | Details |
| D | HIS177 | |
| D | HIS110 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1gtp |
| Chain | Residue | Details |
| E | HIS177 | |
| E | HIS110 |
