6KGY
HOCl-induced flavoprotein disulfide reductase RclA from Escherichia coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0008823 | molecular_function | cupric reductase (NADH) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| A | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 1901530 | biological_process | response to hypochlorite |
| B | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0008823 | molecular_function | cupric reductase (NADH) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| B | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 1901530 | biological_process | response to hypochlorite |
| C | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| C | 0006979 | biological_process | response to oxidative stress |
| C | 0008823 | molecular_function | cupric reductase (NADH) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| C | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 1901530 | biological_process | response to hypochlorite |
| D | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| D | 0006979 | biological_process | response to oxidative stress |
| D | 0008823 | molecular_function | cupric reductase (NADH) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| D | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 1901530 | biological_process | response to hypochlorite |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | GLY10 |
| A | CYS48 |
| A | THR51 |
| A | LYS52 |
| A | ALA99 |
| A | ASN126 |
| A | THR127 |
| A | GLY128 |
| A | ARG252 |
| A | SER258 |
| A | LEU259 |
| A | GLY12 |
| A | ASP292 |
| A | GLN298 |
| A | PHE299 |
| A | THR300 |
| A | TYR301 |
| A | SER303 |
| B | HIS426 |
| A | LYS13 |
| A | GLU33 |
| A | GLN34 |
| A | GLY41 |
| A | THR42 |
| A | CYS43 |
| A | GLY47 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| A | HIS426 |
| B | ILE9 |
| B | GLY10 |
| B | GLY12 |
| B | LYS13 |
| B | GLU33 |
| B | GLN34 |
| B | MET38 |
| B | GLY41 |
| B | THR42 |
| B | CYS43 |
| B | CYS48 |
| B | LYS52 |
| B | ALA99 |
| B | ASN126 |
| B | THR127 |
| B | GLY128 |
| B | ILE169 |
| B | ARG252 |
| B | GLY291 |
| B | ASP292 |
| B | GLN298 |
| B | PHE299 |
| B | THR300 |
| B | TYR301 |
| B | SER303 |
| B | PHE333 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 502 |
| Chain | Residue |
| B | ASN327 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | binding site for residue FAD C 501 |
| Chain | Residue |
| C | ILE9 |
| C | GLY10 |
| C | GLY12 |
| C | LYS13 |
| C | ILE32 |
| C | GLU33 |
| C | GLN34 |
| C | MET38 |
| C | GLY41 |
| C | THR42 |
| C | CYS43 |
| C | ILE46 |
| C | GLY47 |
| C | CYS48 |
| C | LYS52 |
| C | GLN98 |
| C | ALA99 |
| C | ASN126 |
| C | THR127 |
| C | GLY128 |
| C | ARG252 |
| C | SER258 |
| C | GLY291 |
| C | ASP292 |
| C | GLN298 |
| C | PHE299 |
| C | THR300 |
| C | TYR301 |
| C | SER303 |
| C | PHE333 |
| D | HIS426 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue CL C 502 |
| Chain | Residue |
| C | HIS105 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue CL C 503 |
| Chain | Residue |
| C | ASN327 |
| site_id | AC7 |
| Number of Residues | 27 |
| Details | binding site for residue FAD D 501 |
| Chain | Residue |
| D | LYS52 |
| D | ALA99 |
| D | ASN126 |
| D | THR127 |
| D | GLY128 |
| D | ILE169 |
| D | ARG252 |
| D | SER258 |
| D | LEU259 |
| D | GLY291 |
| D | ASP292 |
| D | GLN298 |
| D | PHE299 |
| D | THR300 |
| D | SER303 |
| C | HIS426 |
| D | ILE9 |
| D | GLY10 |
| D | GLY12 |
| D | LYS13 |
| D | GLU33 |
| D | GLN34 |
| D | MET38 |
| D | THR42 |
| D | CYS43 |
| D | GLY47 |
| D | CYS48 |
Functional Information from PROSITE/UniProt
| site_id | PS00076 |
| Number of Residues | 11 |
| Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCIniGCIP |
| Chain | Residue | Details |
| A | GLY40-PRO50 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
