3QNA
Crystal structure of a 6-pyruvoyltetrahydropterin synthase homologue from Esherichia coli complexed sepiapterin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008616 | biological_process | queuosine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070497 | molecular_function | 6-carboxy-5,6,7,8-tetrahydropterin synthase activity |
| B | 0008616 | biological_process | queuosine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070497 | molecular_function | 6-carboxy-5,6,7,8-tetrahydropterin synthase activity |
| C | 0008616 | biological_process | queuosine biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070497 | molecular_function | 6-carboxy-5,6,7,8-tetrahydropterin synthase activity |
| D | 0008616 | biological_process | queuosine biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0070497 | molecular_function | 6-carboxy-5,6,7,8-tetrahydropterin synthase activity |
| E | 0008616 | biological_process | queuosine biosynthetic process |
| E | 0016829 | molecular_function | lyase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0070497 | molecular_function | 6-carboxy-5,6,7,8-tetrahydropterin synthase activity |
| F | 0008616 | biological_process | queuosine biosynthetic process |
| F | 0016829 | molecular_function | lyase activity |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0070497 | molecular_function | 6-carboxy-5,6,7,8-tetrahydropterin synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE BIO A 121 |
| Chain | Residue |
| A | HIS15 |
| A | GLU109 |
| A | ZN122 |
| B | LEU5 |
| B | TRP50 |
| B | ILE52 |
| B | ASP53 |
| B | PHE54 |
| D | HIS70 |
| A | LEU17 |
| A | LYS25 |
| A | ALA26 |
| A | HIS30 |
| A | HIS32 |
| A | THR83 |
| A | SER84 |
| A | GLU85 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 122 |
| Chain | Residue |
| A | HIS15 |
| A | HIS30 |
| A | HIS32 |
| A | BIO121 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE BIO B 121 |
| Chain | Residue |
| B | HIS15 |
| B | LYS25 |
| B | ALA26 |
| B | HIS30 |
| B | HIS32 |
| B | THR83 |
| B | SER84 |
| B | GLU85 |
| B | GLU109 |
| B | ZN122 |
| C | LEU5 |
| C | TRP50 |
| C | ILE52 |
| C | ASP53 |
| C | PHE54 |
| F | HIS70 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 122 |
| Chain | Residue |
| B | HIS15 |
| B | HIS30 |
| B | HIS32 |
| B | BIO121 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BIO C 121 |
| Chain | Residue |
| A | TRP50 |
| A | ILE52 |
| A | ASP53 |
| A | PHE54 |
| C | HIS15 |
| C | LEU17 |
| C | ALA26 |
| C | HIS30 |
| C | HIS32 |
| C | THR83 |
| C | SER84 |
| C | GLU85 |
| C | GLU109 |
| C | ZN122 |
| E | HIS70 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 122 |
| Chain | Residue |
| C | HIS15 |
| C | HIS30 |
| C | HIS32 |
| C | BIO121 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE BIO D 121 |
| Chain | Residue |
| A | HIS70 |
| D | HIS15 |
| D | LYS25 |
| D | ALA26 |
| D | HIS30 |
| D | HIS32 |
| D | THR83 |
| D | SER84 |
| D | GLU85 |
| D | GLU109 |
| D | ZN122 |
| E | LEU5 |
| E | TRP50 |
| E | ILE52 |
| E | ASP53 |
| E | PHE54 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 122 |
| Chain | Residue |
| D | HIS15 |
| D | HIS30 |
| D | HIS32 |
| D | BIO121 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BIO E 121 |
| Chain | Residue |
| C | HIS70 |
| E | HIS15 |
| E | ALA26 |
| E | HIS30 |
| E | HIS32 |
| E | THR83 |
| E | SER84 |
| E | GLU85 |
| E | GLU109 |
| E | ZN122 |
| F | TRP50 |
| F | ILE52 |
| F | ASP53 |
| F | PHE54 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 122 |
| Chain | Residue |
| E | HIS15 |
| E | HIS30 |
| E | HIS32 |
| E | BIO121 |
| site_id | BC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE BIO F 121 |
| Chain | Residue |
| D | LEU5 |
| D | TRP50 |
| D | ILE52 |
| D | ASP53 |
| D | PHE54 |
| F | HIS15 |
| F | LEU17 |
| F | LYS25 |
| F | ALA26 |
| F | HIS30 |
| F | HIS32 |
| F | THR83 |
| F | SER84 |
| F | GLU85 |
| F | GLU109 |
| F | ZN122 |
| B | HIS70 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN F 122 |
| Chain | Residue |
| F | HIS15 |
| F | HIS30 |
| F | HIS32 |
| F | GLU109 |
| F | BIO121 |
