Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0006400 | biological_process | tRNA modification |
| A | 0008033 | biological_process | tRNA processing |
| A | 0045301 | molecular_function | tRNA-(2-methylthio-N-6-(cis-hydroxy)isopentenyl adenosine)-hydroxylase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0006400 | biological_process | tRNA modification |
| B | 0008033 | biological_process | tRNA processing |
| B | 0045301 | molecular_function | tRNA-(2-methylthio-N-6-(cis-hydroxy)isopentenyl adenosine)-hydroxylase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FE A 501 |
| Chain | Residue |
| A | GLU38 |
| A | GLU69 |
| A | HIS72 |
| A | GLU151 |
| A | FE502 |
| A | PER503 |
| A | HOH511 |
| A | HOH512 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE A 502 |
| Chain | Residue |
| A | GLU69 |
| A | GLU122 |
| A | GLU151 |
| A | HIS154 |
| A | FE501 |
| A | PER503 |
| A | HOH512 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE B 501 |
| Chain | Residue |
| B | GLU38 |
| B | GLU69 |
| B | HIS72 |
| B | GLU151 |
| B | FE502 |
| B | UNL503 |
| B | HOH514 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 502 |
| Chain | Residue |
| B | GLU69 |
| B | GLU122 |
| B | GLU151 |
| B | HIS154 |
| B | FE501 |
| B | UNL503 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PER A 503 |
| Chain | Residue |
| A | GLU38 |
| A | GLU69 |
| A | GLU122 |
| A | GLU151 |
| A | FE501 |
| A | FE502 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE UNL B 503 |
| Chain | Residue |
| B | CYS37 |
| B | GLU38 |
| B | ALA41 |
| B | GLU69 |
| B | GLU122 |
| B | GLU151 |
| B | FE501 |
| B | FE502 |
| B | EDO510 |
| B | HOH514 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 504 |
| Chain | Residue |
| B | CYS37 |
| B | HIS196 |
| B | HOH595 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 505 |
| Chain | Residue |
| B | GLY12 |
| B | GLN75 |
| B | ARG78 |
| B | ARG82 |
| B | PHE143 |
| B | MSE183 |
| B | HOH522 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 504 |
| Chain | Residue |
| A | LEU102 |
| A | ARG104 |
| A | ASP113 |
| A | CYS174 |
| A | HOH519 |
| A | HOH551 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 506 |
| Chain | Residue |
| B | ASN36 |
| B | EDO513 |
| B | HOH531 |
| B | HOH567 |
| B | HOH620 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 505 |
| Chain | Residue |
| A | HIS55 |
| A | HOH531 |
| B | ALA169 |
| B | ARG173 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 506 |
| Chain | Residue |
| A | THR44 |
| A | ARG100 |
| A | THR114 |
| A | VAL117 |
| A | GLY118 |
| A | ILE121 |
| A | EDO510 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 507 |
| Chain | Residue |
| B | ASN164 |
| B | GLY166 |
| B | ASP167 |
| A | ASN53 |
| B | PRO89 |
| B | HIS163 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 508 |
| Chain | Residue |
| B | LEU102 |
| B | ARG104 |
| B | ASP113 |
| B | LEU177 |
| B | HOH546 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 509 |
| Chain | Residue |
| B | ASP33 |
| B | ASN36 |
| B | LYS40 |
| B | ALA92 |
| B | GLY93 |
| B | HOH517 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 510 |
| Chain | Residue |
| B | THR44 |
| B | GLU69 |
| B | GLU122 |
| B | TYR158 |
| B | UNL503 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 507 |
| Chain | Residue |
| A | ASP33 |
| A | ASN36 |
| A | CYS37 |
| A | ALA92 |
| A | GLY93 |
| A | HOH526 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 511 |
| Chain | Residue |
| B | GLN75 |
| B | PHE143 |
| B | GLY146 |
| B | MSE183 |
| B | GLN187 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 512 |
| Chain | Residue |
| A | GLU107 |
| B | ARG82 |
| B | ALA172 |
| B | GLU176 |
| B | ARG179 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 508 |
| Chain | Residue |
| A | LYS35 |
| A | ASN36 |
| A | HIS73 |
| A | HOH532 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 509 |
| Chain | Residue |
| A | ASP170 |
| A | ARG173 |
| B | ARG83 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 513 |
| Chain | Residue |
| A | ILE49 |
| A | ASN53 |
| B | LYS35 |
| B | HIS73 |
| B | EDO506 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 510 |
| Chain | Residue |
| A | GLU122 |
| A | TYR158 |
| A | EDO506 |
| A | HOH535 |
| site_id | FEA |
| Number of Residues | 10 |
| Details | DI-IRON METAL BINDING SITE FROM CHAIN A. A PEROXIDE ION (PER A503) WAS MODELED BRIDGING THE TWO IRON ATOMS. THE ASSIGNMENT OF THE PEROXIDE ION IS TENTATIVE AND IS BASED ON THE ENZYME FUNCTION AND THE ELECTRON DENSITY. HOWEVER, WE DON'T HAVE SPECTROSCOPIC DATA AT THIS TIME. |
| Chain | Residue |
| A | GLU38 |
| A | HOH512 |
| A | GLU69 |
| A | HIS72 |
| A | GLU122 |
| A | HIS154 |
| A | FE501 |
| A | FE502 |
| A | PER503 |
| A | HOH511 |
| site_id | FEB |
| Number of Residues | 10 |
| Details | DI-IRON METAL BINDING SITE FROM CHAIN B. NOTE THAT SITE FEB DIFFERS FROM SITE FEA. THE DENSITY FOR THE MODELED UNKNOWN LIAGND (UNL) DIFFERS FROM THE NCS DENSITY IN SITE FEA THAT WAS MODELED AS A PEROXIDE ION. |
| Chain | Residue |
| B | GLU38 |
| B | GLU69 |
| B | HIS72 |
| B | GLU122 |
| B | GLU151 |
| B | HIS154 |
| B | FE501 |
| B | FE502 |
| B | UNL503 |
| B | HOH514 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | GLU38 | |
| A | GLU69 | |
| A | HIS72 | |
| A | GLU122 | |
| A | HIS154 | |
| B | GLU38 | |
| B | GLU69 | |
| B | HIS72 | |
| B | GLU122 | |
| B | HIS154 | |
| Chain | Residue | Details |
| A | GLU151 | |
| B | GLU151 | |
