1XDQ
Structural and Biochemical Identification of a Novel Bacterial Oxidoreductase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016667 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors |
| A | 0016672 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor |
| A | 0016675 | molecular_function | oxidoreductase activity, acting on a heme group of donors |
| A | 0030091 | biological_process | protein repair |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0043546 | molecular_function | molybdopterin cofactor binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0055114 | biological_process | obsolete oxidation-reduction process |
| A | 1901530 | biological_process | response to hypochlorite |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016667 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors |
| B | 0016672 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor |
| B | 0016675 | molecular_function | oxidoreductase activity, acting on a heme group of donors |
| B | 0030091 | biological_process | protein repair |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0043546 | molecular_function | molybdopterin cofactor binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0055114 | biological_process | obsolete oxidation-reduction process |
| B | 1901530 | biological_process | response to hypochlorite |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016667 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors |
| C | 0016672 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor |
| C | 0016675 | molecular_function | oxidoreductase activity, acting on a heme group of donors |
| C | 0030091 | biological_process | protein repair |
| C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0043546 | molecular_function | molybdopterin cofactor binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0055114 | biological_process | obsolete oxidation-reduction process |
| C | 1901530 | biological_process | response to hypochlorite |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016667 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors |
| D | 0016672 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor |
| D | 0016675 | molecular_function | oxidoreductase activity, acting on a heme group of donors |
| D | 0030091 | biological_process | protein repair |
| D | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0043546 | molecular_function | molybdopterin cofactor binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0055114 | biological_process | obsolete oxidation-reduction process |
| D | 1901530 | biological_process | response to hypochlorite |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016667 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors |
| E | 0016672 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor |
| E | 0016675 | molecular_function | oxidoreductase activity, acting on a heme group of donors |
| E | 0030091 | biological_process | protein repair |
| E | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| E | 0042597 | cellular_component | periplasmic space |
| E | 0043546 | molecular_function | molybdopterin cofactor binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0055114 | biological_process | obsolete oxidation-reduction process |
| E | 1901530 | biological_process | response to hypochlorite |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE URE A 401 |
| Chain | Residue |
| A | TYR47 |
| A | GLU104 |
| A | TRP223 |
| A | TYR231 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE URE B 402 |
| Chain | Residue |
| B | HOH628 |
| B | TYR47 |
| B | GLU104 |
| B | TRP223 |
| B | TYR231 |
| B | ARG245 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE URE C 403 |
| Chain | Residue |
| C | TYR47 |
| C | GLU104 |
| C | TRP223 |
| C | TYR231 |
| C | ARG245 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE URE D 404 |
| Chain | Residue |
| D | TYR47 |
| D | GLU104 |
| D | TRP223 |
| D | TYR231 |
| D | ARG245 |
| D | HOH629 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE URE E 405 |
| Chain | Residue |
| E | TYR47 |
| E | GLU104 |
| E | TRP223 |
| E | TYR231 |
| E | HOH630 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MO A 501 |
| Chain | Residue |
| A | ASN45 |
| A | CYS102 |
| A | MTE301 |
| A | O601 |
| A | HOH645 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MO B 502 |
| Chain | Residue |
| B | ASN45 |
| B | CYS102 |
| B | MTE302 |
| B | O602 |
| B | HOH628 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MO C 503 |
| Chain | Residue |
| C | CYS102 |
| C | MTE303 |
| C | O603 |
| C | HOH621 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MO D 504 |
| Chain | Residue |
| D | CYS102 |
| D | MTE304 |
| D | O604 |
| D | HOH629 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MO E 505 |
| Chain | Residue |
| E | ASN45 |
| E | CYS102 |
| E | MTE305 |
| E | O605 |
| E | HOH630 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE O A 601 |
| Chain | Residue |
| A | CYS102 |
| A | VAL103 |
| A | GLY202 |
| A | PHE203 |
| A | MTE301 |
| A | MO501 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE O B 602 |
| Chain | Residue |
| B | CYS102 |
| B | VAL103 |
| B | GLY202 |
| B | PHE203 |
| B | MTE302 |
| B | MO502 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE O C 603 |
| Chain | Residue |
| C | CYS102 |
| C | VAL103 |
| C | GLY202 |
| C | PHE203 |
| C | MTE303 |
| C | MO503 |
| C | HOH621 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE O D 604 |
| Chain | Residue |
| D | CYS102 |
| D | VAL103 |
| D | GLY202 |
| D | PHE203 |
| D | MTE304 |
| D | MO504 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE O E 605 |
| Chain | Residue |
| E | CYS102 |
| E | VAL103 |
| E | GLY202 |
| E | PHE203 |
| E | MTE305 |
| E | MO505 |
| site_id | BC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE MTE A 301 |
| Chain | Residue |
| A | ASN44 |
| A | ASN45 |
| A | PHE46 |
| A | TYR47 |
| A | GLU48 |
| A | CYS102 |
| A | MET108 |
| A | THR137 |
| A | TYR160 |
| A | ASN189 |
| A | ARG194 |
| A | GLY202 |
| A | GLY205 |
| A | LYS207 |
| A | MO501 |
| A | O601 |
| A | HOH645 |
| site_id | BC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE MTE B 302 |
| Chain | Residue |
| B | PHE46 |
| B | TYR47 |
| B | GLU48 |
| B | CYS102 |
| B | MET108 |
| B | THR137 |
| B | TYR160 |
| B | ASN189 |
| B | ARG194 |
| B | GLY202 |
| B | PHE203 |
| B | GLY205 |
| B | LYS207 |
| B | MO502 |
| B | O602 |
| B | ASN44 |
| B | ASN45 |
| site_id | BC9 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE MTE C 303 |
| Chain | Residue |
| C | ASN44 |
| C | ASN45 |
| C | PHE46 |
| C | TYR47 |
| C | GLU48 |
| C | CYS102 |
| C | MET108 |
| C | THR137 |
| C | TYR160 |
| C | ASN189 |
| C | ARG194 |
| C | GLY202 |
| C | PHE203 |
| C | GLY205 |
| C | LYS207 |
| C | MO503 |
| C | O603 |
| C | HOH621 |
| site_id | CC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE MTE D 304 |
| Chain | Residue |
| D | ASN44 |
| D | ASN45 |
| D | PHE46 |
| D | TYR47 |
| D | GLU48 |
| D | CYS102 |
| D | MET108 |
| D | THR137 |
| D | TYR160 |
| D | ASN189 |
| D | ARG194 |
| D | GLY202 |
| D | PHE203 |
| D | GLY205 |
| D | LYS207 |
| D | MO504 |
| D | O604 |
| D | HOH629 |
| site_id | CC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE MTE E 305 |
| Chain | Residue |
| E | ASN44 |
| E | ASN45 |
| E | PHE46 |
| E | TYR47 |
| E | GLU48 |
| E | CYS102 |
| E | MET108 |
| E | THR137 |
| E | TYR160 |
| E | ASN189 |
| E | ARG194 |
| E | GLY202 |
| E | PHE203 |
| E | GLY205 |
| E | LYS207 |
| E | MO505 |
| E | O605 |
| E | HOH630 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 35 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15355966 |
| Chain | Residue | Details |
| A | ASN44 | |
| B | CYS102 | |
| B | THR137 | |
| B | ASN189 | |
| B | ARG194 | |
| B | GLY205 | |
| C | ASN44 | |
| C | TYR47 | |
| C | CYS102 | |
| C | THR137 | |
| C | ASN189 | |
| A | TYR47 | |
| C | ARG194 | |
| C | GLY205 | |
| D | ASN44 | |
| D | TYR47 | |
| D | CYS102 | |
| D | THR137 | |
| D | ASN189 | |
| D | ARG194 | |
| D | GLY205 | |
| E | ASN44 | |
| A | CYS102 | |
| E | TYR47 | |
| E | CYS102 | |
| E | THR137 | |
| E | ASN189 | |
| E | ARG194 | |
| E | GLY205 | |
| A | THR137 | |
| A | ASN189 | |
| A | ARG194 | |
| A | GLY205 | |
| B | ASN44 | |
| B | TYR47 |
