6KYY
Cu(II) complex of HOCl-induced flavoprotein disulfide reductase RclA from Escherichia coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 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 | 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 | 29 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | GLY10 |
| A | THR42 |
| A | CYS43 |
| A | CYS48 |
| A | LYS52 |
| A | GLY97 |
| A | ALA99 |
| A | ASN126 |
| A | THR127 |
| A | GLY128 |
| A | ILE169 |
| A | PHE11 |
| A | ARG252 |
| A | LEU259 |
| A | GLY291 |
| A | ASP292 |
| A | GLN298 |
| A | PHE299 |
| A | THR300 |
| A | TYR301 |
| A | SER303 |
| B | HIS426 |
| A | GLY12 |
| A | LYS13 |
| A | ILE32 |
| A | GLU33 |
| A | GLN34 |
| A | MET38 |
| A | GLY41 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue CU A 502 |
| Chain | Residue |
| A | HIS61 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue CU A 503 |
| Chain | Residue |
| A | HIS84 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CU A 504 |
| Chain | Residue |
| A | HIS235 |
| A | HIS238 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CU A 505 |
| Chain | Residue |
| A | HIS160 |
| A | ALA242 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue CU A 506 |
| Chain | Residue |
| A | HIS110 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue CU A 507 |
| Chain | Residue |
| A | HIS119 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue CU A 508 |
| Chain | Residue |
| A | SER258 |
| A | HIS260 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue CU A 509 |
| Chain | Residue |
| A | CYS43 |
| A | CYS48 |
| A | THR300 |
| B | HIS426 |
| site_id | AD1 |
| Number of Residues | 27 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| A | HIS426 |
| B | GLY10 |
| B | GLY12 |
| B | LYS13 |
| B | GLU33 |
| B | GLN34 |
| B | MET38 |
| B | THR42 |
| B | CYS43 |
| B | CYS48 |
| B | LYS52 |
| B | GLN98 |
| B | ALA99 |
| B | ASN126 |
| B | THR127 |
| B | GLY128 |
| B | SER148 |
| B | ILE169 |
| B | ARG252 |
| B | GLY291 |
| B | ASP292 |
| B | GLN298 |
| B | PHE299 |
| B | THR300 |
| B | TYR301 |
| B | SER303 |
| B | PHE333 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue CU B 502 |
| Chain | Residue |
| B | HIS105 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue CU B 503 |
| Chain | Residue |
| B | HIS260 |
| site_id | AD4 |
| Number of Residues | 1 |
| Details | binding site for residue CU B 504 |
| Chain | Residue |
| B | HIS61 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue CU B 505 |
| Chain | Residue |
| B | ASN80 |
| B | HIS84 |
| site_id | AD6 |
| Number of Residues | 1 |
| Details | binding site for residue CU B 506 |
| Chain | Residue |
| B | HIS221 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue CU B 507 |
| Chain | Residue |
| B | HIS238 |
| D | GLU156 |
| site_id | AD8 |
| Number of Residues | 1 |
| Details | binding site for residue CU B 508 |
| Chain | Residue |
| B | HIS235 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue CU B 509 |
| Chain | Residue |
| A | HIS426 |
| B | CYS43 |
| B | CYS48 |
| B | THR300 |
| site_id | AE1 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 510 |
| Chain | Residue |
| B | ASN327 |
| site_id | AE2 |
| Number of Residues | 2 |
| Details | binding site for residue CU C 501 |
| Chain | Residue |
| B | ARG108 |
| C | ASN327 |
| site_id | AE3 |
| Number of Residues | 29 |
| Details | binding site for residue FAD C 502 |
| Chain | Residue |
| C | LYS52 |
| C | GLN98 |
| C | ALA99 |
| C | ASN126 |
| C | THR127 |
| C | GLY128 |
| C | ILE169 |
| C | ARG252 |
| C | GLY291 |
| C | ASP292 |
| C | GLN298 |
| C | PHE299 |
| C | THR300 |
| C | TYR301 |
| C | SER303 |
| D | HIS426 |
| C | ILE9 |
| C | GLY10 |
| C | GLY12 |
| C | LYS13 |
| C | GLU33 |
| C | GLN34 |
| C | MET38 |
| C | GLY41 |
| C | THR42 |
| C | CYS43 |
| C | ILE46 |
| C | GLY47 |
| C | CYS48 |
| site_id | AE4 |
| Number of Residues | 1 |
| Details | binding site for residue CU C 503 |
| Chain | Residue |
| C | HIS105 |
| site_id | AE5 |
| Number of Residues | 1 |
| Details | binding site for residue CU C 504 |
| Chain | Residue |
| C | HIS227 |
| site_id | AE6 |
| Number of Residues | 1 |
| Details | binding site for residue CU C 505 |
| Chain | Residue |
| C | HIS221 |
| site_id | AE7 |
| Number of Residues | 1 |
| Details | binding site for residue CU C 506 |
| Chain | Residue |
| C | HIS260 |
| site_id | AE8 |
| Number of Residues | 1 |
| Details | binding site for residue CU C 507 |
| Chain | Residue |
| C | HIS61 |
| site_id | AE9 |
| Number of Residues | 2 |
| Details | binding site for residue CU C 508 |
| Chain | Residue |
| C | ASN80 |
| C | HIS84 |
| site_id | AF1 |
| Number of Residues | 2 |
| Details | binding site for residue CU C 509 |
| Chain | Residue |
| B | HIS105 |
| C | GLY352 |
| site_id | AF2 |
| Number of Residues | 1 |
| Details | binding site for residue CL C 510 |
| Chain | Residue |
| C | TYR168 |
| site_id | AF3 |
| Number of Residues | 1 |
| Details | binding site for residue CU C 511 |
| Chain | Residue |
| C | HIS228 |
| site_id | AF4 |
| Number of Residues | 29 |
| Details | binding site for residue FAD D 501 |
| Chain | Residue |
| C | HIS426 |
| D | ILE9 |
| D | GLY10 |
| D | GLY12 |
| D | LYS13 |
| D | ILE32 |
| D | GLU33 |
| D | GLN34 |
| D | MET38 |
| D | GLY41 |
| D | THR42 |
| D | CYS43 |
| D | GLY47 |
| D | CYS48 |
| D | LYS52 |
| D | ALA99 |
| D | ASN126 |
| D | THR127 |
| D | GLY128 |
| D | ILE169 |
| D | ARG252 |
| D | SER258 |
| D | GLY291 |
| D | ASP292 |
| D | GLN298 |
| D | PHE299 |
| D | THR300 |
| D | TYR301 |
| D | SER303 |
| site_id | AF5 |
| Number of Residues | 1 |
| Details | binding site for residue CU D 502 |
| Chain | Residue |
| D | HIS260 |
| site_id | AF6 |
| Number of Residues | 1 |
| Details | binding site for residue CU D 503 |
| Chain | Residue |
| D | HIS110 |
| site_id | AF7 |
| Number of Residues | 1 |
| Details | binding site for residue CU D 504 |
| Chain | Residue |
| D | HIS227 |
| site_id | AF8 |
| Number of Residues | 1 |
| Details | binding site for residue CU D 505 |
| Chain | Residue |
| D | HIS61 |
| site_id | AF9 |
| Number of Residues | 2 |
| Details | binding site for residue CU D 506 |
| Chain | Residue |
| D | HIS56 |
| D | GLN60 |
| site_id | AG1 |
| Number of Residues | 1 |
| Details | binding site for residue CU D 507 |
| Chain | Residue |
| D | HIS84 |
| site_id | AG2 |
| Number of Residues | 4 |
| Details | binding site for residue CU D 508 |
| Chain | Residue |
| C | HIS426 |
| D | CYS43 |
| D | CYS48 |
| D | THR300 |
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 | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS426 | |
| B | HIS426 | |
| C | HIS426 | |
| D | HIS426 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU33 | |
| B | GLU33 | |
| C | GLU33 | |
| D | GLU33 |
