3QN0
Structure of 6-pyruvoyltetrahydropterin synthase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0070497 | molecular_function | 6-carboxytetrahydropterin synthase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0070497 | molecular_function | 6-carboxytetrahydropterin synthase activity |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0070497 | molecular_function | 6-carboxytetrahydropterin synthase activity |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0070497 | molecular_function | 6-carboxytetrahydropterin synthase activity |
| E | 0008270 | molecular_function | zinc ion binding |
| E | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0070497 | molecular_function | 6-carboxytetrahydropterin synthase activity |
| F | 0008270 | molecular_function | zinc ion binding |
| F | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0070497 | molecular_function | 6-carboxytetrahydropterin synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 121 |
| Chain | Residue |
| A | HIS15 |
| A | HIS30 |
| A | HIS32 |
| A | GLU109 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 121 |
| Chain | Residue |
| B | HIS15 |
| B | HIS30 |
| B | HIS32 |
| B | GLU109 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 121 |
| Chain | Residue |
| C | HIS30 |
| C | HIS32 |
| C | GLU109 |
| C | HIS15 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 121 |
| Chain | Residue |
| D | HIS15 |
| D | HIS30 |
| D | HIS32 |
| D | GLU109 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 121 |
| Chain | Residue |
| E | HIS15 |
| E | HIS30 |
| E | HIS32 |
| E | GLU109 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN F 121 |
| Chain | Residue |
| B | HOH122 |
| F | HIS15 |
| F | HIS30 |
| F | HIS32 |
| F | GLU109 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"24990950","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24816091","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24990950","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QN0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QN9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QNA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NTK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NTM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NTN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"description":"in chain A","evidences":[{"source":"PubMed","id":"24816091","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24990950","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QNA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NTK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in chain A","evidences":[{"source":"PubMed","id":"24990950","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NTK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in chain C","evidences":[{"source":"PubMed","id":"24990950","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NTK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | Binding site: {"description":"in chain B","evidences":[{"source":"PubMed","id":"24816091","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24990950","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QNA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NTK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in chain B","evidences":[{"source":"PubMed","id":"24990950","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NTK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 12 |
| Details | Site: {"description":"Increases basicity of active site Cys","evidences":[{"source":"PubMed","id":"24990950","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 12 |
| Details | Site: {"description":"Key residue that determines the differing bacterial enzyme with CTPS activity from the mammalian homolog with PTPS (6-pyruvoyltetrahydropterin synthase) activity","evidences":[{"source":"PubMed","id":"24816091","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
