2IFA
Crystal Structure of the PUTATIVE NITROREDUCTASE (SMU.260) IN COMPLEX WITH FMN FROM STREPTOCOCCUS MUTANS, NORTHEAST STRUCTURAL GENOMICS TARGET SMR5.
Replaces: 1YW3Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0034599 | biological_process | cellular response to oxidative stress |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0034599 | biological_process | cellular response to oxidative stress |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0034599 | biological_process | cellular response to oxidative stress |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0034599 | biological_process | cellular response to oxidative stress |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FMN A 501 |
| Chain | Residue |
| A | ARG11 |
| A | HOH509 |
| A | HOH529 |
| A | HOH578 |
| A | HOH617 |
| B | PRO40 |
| B | SER41 |
| B | ALA42 |
| B | PHE43 |
| B | ASN44 |
| B | TRP122 |
| A | ARG12 |
| B | GLN125 |
| B | ILE129 |
| D | ASN107 |
| D | GLU110 |
| D | ASN111 |
| D | HOH572 |
| A | SER13 |
| A | TYR15 |
| A | TRP135 |
| A | VAL147 |
| A | GLN148 |
| A | HIS149 |
| A | LYS186 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN B 502 |
| Chain | Residue |
| A | PRO40 |
| A | SER41 |
| A | ALA42 |
| A | PHE43 |
| A | ASN44 |
| A | TRP122 |
| A | GLN125 |
| A | ILE129 |
| B | ARG11 |
| B | ARG12 |
| B | SER13 |
| B | TYR15 |
| B | VAL147 |
| B | GLN148 |
| B | HIS149 |
| B | LYS186 |
| B | HOH515 |
| B | HOH605 |
| E | HOH536 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FMN C 503 |
| Chain | Residue |
| B | ASN111 |
| B | HOH537 |
| C | ARG11 |
| C | ARG12 |
| C | SER13 |
| C | TYR15 |
| C | VAL147 |
| C | GLN148 |
| C | HIS149 |
| C | LYS186 |
| C | HOH546 |
| C | HOH569 |
| D | PRO40 |
| D | SER41 |
| D | ALA42 |
| D | PHE43 |
| D | ASN44 |
| D | TRP122 |
| D | GLN125 |
| D | ILE129 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN D 504 |
| Chain | Residue |
| C | PRO40 |
| C | SER41 |
| C | ALA42 |
| C | PHE43 |
| C | ASN44 |
| C | TRP122 |
| C | GLN125 |
| C | ILE129 |
| D | ARG11 |
| D | ARG12 |
| D | SER13 |
| D | TYR15 |
| D | TRP135 |
| D | VAL147 |
| D | GLN148 |
| D | HIS149 |
| D | LYS186 |
| D | HOH525 |
| F | ASN107 |
| F | GLU110 |
| F | ASN111 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FMN E 505 |
| Chain | Residue |
| F | PRO40 |
| F | SER41 |
| F | ALA42 |
| F | PHE43 |
| F | ASN44 |
| F | TRP122 |
| F | GLN125 |
| F | ILE129 |
| C | ASN107 |
| C | GLU110 |
| C | ASN111 |
| E | ARG11 |
| E | ARG12 |
| E | SER13 |
| E | TYR15 |
| E | VAL147 |
| E | GLN148 |
| E | HIS149 |
| E | LYS186 |
| E | HOH506 |
| E | HOH509 |
| E | HOH557 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN F 506 |
| Chain | Residue |
| A | GLU110 |
| A | ASN111 |
| E | PRO40 |
| E | SER41 |
| E | ALA42 |
| E | PHE43 |
| E | ASN44 |
| E | TRP122 |
| E | GLN125 |
| E | ILE129 |
| F | ARG11 |
| F | ARG12 |
| F | SER13 |
| F | TYR15 |
| F | TRP135 |
| F | VAL147 |
| F | HIS149 |
| F | LYS186 |
| F | HOH517 |
| F | HOH527 |
| F | HOH542 |
