6Z88
human GTP cyclohydrolase I in complex with allosteric inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003934 | molecular_function | GTP cyclohydrolase I activity |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0003934 | molecular_function | GTP cyclohydrolase I activity |
| B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| C | 0003934 | molecular_function | GTP cyclohydrolase I activity |
| C | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| D | 0003934 | molecular_function | GTP cyclohydrolase I activity |
| D | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| E | 0003934 | molecular_function | GTP cyclohydrolase I activity |
| E | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| F | 0003934 | molecular_function | GTP cyclohydrolase I activity |
| F | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| G | 0003934 | molecular_function | GTP cyclohydrolase I activity |
| G | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| H | 0003934 | molecular_function | GTP cyclohydrolase I activity |
| H | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| I | 0003934 | molecular_function | GTP cyclohydrolase I activity |
| I | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| J | 0003934 | molecular_function | GTP cyclohydrolase I activity |
| J | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue QBK A 301 |
| Chain | Residue |
| A | ASP127 |
| A | MET129 |
| A | LEU157 |
| A | THR240 |
| A | GLU243 |
| E | SER228 |
| E | ARG235 |
| E | ARG241 |
| E | HOH313 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue QBK A 302 |
| Chain | Residue |
| A | SER228 |
| A | MET230 |
| A | ARG235 |
| A | ARG241 |
| C | ASP127 |
| C | MET129 |
| C | LEU157 |
| C | THR240 |
| C | GLU243 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | CYS141 |
| B | HIS144 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue QBK B 302 |
| Chain | Residue |
| B | SER228 |
| B | MET230 |
| B | ARG235 |
| B | ARG241 |
| F | ASP127 |
| F | MET129 |
| F | LEU157 |
| F | THR240 |
| F | GLU243 |
| F | HOH403 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue QBK C 301 |
| Chain | Residue |
| C | SER228 |
| C | MET230 |
| C | ARG235 |
| C | ARG241 |
| C | HOH403 |
| C | HOH406 |
| I | ASP127 |
| I | MET129 |
| I | LEU157 |
| I | THR240 |
| I | GLU243 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue QBK D 301 |
| Chain | Residue |
| B | ASP127 |
| B | LEU157 |
| B | THR240 |
| B | GLU243 |
| D | SER228 |
| D | MET230 |
| D | ARG235 |
| D | ARG241 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue QBK D 302 |
| Chain | Residue |
| D | LEU157 |
| D | THR240 |
| D | GLU243 |
| D | HOH405 |
| H | SER228 |
| H | MET230 |
| H | ARG235 |
| H | ARG241 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue QBK F 302 |
| Chain | Residue |
| F | SER228 |
| F | MET230 |
| F | ARG235 |
| F | ARG241 |
| J | ASP127 |
| J | LEU157 |
| J | THR240 |
| J | GLU243 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue QBK G 301 |
| Chain | Residue |
| E | LEU157 |
| E | THR240 |
| E | GLU243 |
| E | HOH302 |
| G | SER228 |
| G | MET230 |
| G | ARG235 |
| G | ARG241 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue QBK G 302 |
| Chain | Residue |
| G | ASP127 |
| G | MET129 |
| G | LEU157 |
| G | THR240 |
| G | GLU243 |
| G | HOH402 |
| I | SER228 |
| I | MET230 |
| I | ARG235 |
| I | ARG241 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue QBK J 301 |
| Chain | Residue |
| H | ASP127 |
| H | LEU157 |
| H | THR240 |
| H | GLU243 |
| J | SER228 |
| J | MET230 |
| J | ARG235 |
| J | ARG241 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11087827","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17704208","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






