1SB3
Structure of 4-hydroxybenzoyl-CoA reductase from Thauera aromatica
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005506 | molecular_function | iron ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0018525 | molecular_function | 4-hydroxybenzoyl-CoA reductase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0018525 | molecular_function | 4-hydroxybenzoyl-CoA reductase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
B | 0071949 | molecular_function | FAD binding |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0018525 | molecular_function | 4-hydroxybenzoyl-CoA reductase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0051536 | molecular_function | iron-sulfur cluster binding |
C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
D | 0005506 | molecular_function | iron ion binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0018525 | molecular_function | 4-hydroxybenzoyl-CoA reductase activity |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0018525 | molecular_function | 4-hydroxybenzoyl-CoA reductase activity |
E | 0046872 | molecular_function | metal ion binding |
E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
E | 0071949 | molecular_function | FAD binding |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0018525 | molecular_function | 4-hydroxybenzoyl-CoA reductase activity |
F | 0046872 | molecular_function | metal ion binding |
F | 0051536 | molecular_function | iron-sulfur cluster binding |
F | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 1112 |
Chain | Residue |
D | ILE705 |
D | GLU706 |
D | VAL707 |
D | HOH2172 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 E 1113 |
Chain | Residue |
E | ALA26 |
E | LEU28 |
E | GLY45 |
E | HIS46 |
E | TYR141 |
site_id | AC3 |
Number of Residues | 40 |
Details | BINDING SITE FOR RESIDUE PCD A 1920 |
Chain | Residue |
A | GLN214 |
A | GLY243 |
A | GLY244 |
A | PHE245 |
A | GLY246 |
A | THR249 |
A | MET357 |
A | ARG358 |
A | ILE481 |
A | GLY482 |
A | GLN483 |
A | GLY484 |
A | SER485 |
A | SER520 |
A | TYR521 |
A | SER522 |
A | SER523 |
A | ARG524 |
A | VAL525 |
A | THR526 |
A | VAL650 |
A | LYS652 |
A | LEU654 |
A | ASN655 |
A | ALA658 |
A | VAL659 |
A | GLN662 |
A | ALA721 |
A | LYS722 |
A | GLU723 |
A | ALA724 |
A | SER725 |
A | GLU726 |
A | HOH1923 |
A | HOH1965 |
A | HOH2011 |
A | HOH2049 |
A | HOH2071 |
C | GLN99 |
C | CYS137 |
site_id | AC4 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FAD B 1900 |
Chain | Residue |
B | PRO29 |
B | GLY31 |
B | ALA32 |
B | GLY33 |
B | THR34 |
B | ASP35 |
B | LEU36 |
B | LEU53 |
B | LEU78 |
B | VAL101 |
B | ALA102 |
B | ALA110 |
B | THR111 |
B | GLY114 |
B | ASN115 |
B | CYS117 |
B | GLN118 |
B | GLY161 |
B | ASP162 |
B | LEU201 |
B | LEU207 |
B | LYS224 |
B | VAL231 |
B | ASP232 |
B | PHE233 |
B | HOH1932 |
B | HOH1942 |
B | HOH1959 |
B | HOH1969 |
C | GLY44 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 B 1910 |
Chain | Residue |
B | CYS122 |
B | CYS138 |
B | LYS140 |
B | CYS146 |
B | HIS147 |
B | CYS155 |
B | TYR156 |
B | ALA157 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FES C 1907 |
Chain | Residue |
A | MET191 |
C | GLN99 |
C | CYS100 |
C | GLY101 |
C | CYS103 |
C | CYS135 |
C | ARG136 |
C | CYS137 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FES C 1908 |
Chain | Residue |
C | CYS46 |
C | GLY47 |
C | CYS49 |
C | CYS61 |
C | GLY40 |
C | CYS41 |
C | GLY44 |
C | GLU45 |
site_id | AC8 |
Number of Residues | 39 |
Details | BINDING SITE FOR RESIDUE PCD D 1921 |
Chain | Residue |
D | GLN214 |
D | GLY243 |
D | GLY244 |
D | PHE245 |
D | GLY246 |
D | THR249 |
D | MET357 |
D | ARG358 |
D | ILE481 |
D | GLY482 |
D | GLN483 |
D | GLY484 |
D | SER485 |
D | SER520 |
D | TYR521 |
D | SER522 |
D | SER523 |
D | ARG524 |
D | VAL525 |
D | THR526 |
D | VAL650 |
D | LYS652 |
D | LEU654 |
D | ASN655 |
D | ALA658 |
D | VAL659 |
D | GLN662 |
D | ALA721 |
D | LYS722 |
D | GLU723 |
D | ALA724 |
D | SER725 |
D | GLU726 |
D | HOH1937 |
D | HOH1962 |
D | HOH2014 |
D | HOH2045 |
F | GLN99 |
F | CYS137 |
site_id | AC9 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FAD E 1901 |
Chain | Residue |
E | PRO29 |
E | GLY31 |
E | ALA32 |
E | GLY33 |
E | THR34 |
E | ASP35 |
E | LEU36 |
E | LEU53 |
E | LEU78 |
E | VAL101 |
E | ALA102 |
E | THR111 |
E | GLY114 |
E | ASN115 |
E | CYS117 |
E | GLN118 |
E | GLY161 |
E | ASP162 |
E | LEU201 |
E | LEU206 |
E | LEU207 |
E | LYS224 |
E | VAL231 |
E | ASP232 |
E | PHE233 |
E | HOH1918 |
E | HOH1928 |
E | HOH1965 |
E | HOH2007 |
F | GLY44 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 E 1911 |
Chain | Residue |
E | CYS122 |
E | PHE124 |
E | CYS138 |
E | LYS140 |
E | CYS146 |
E | HIS147 |
E | CYS155 |
E | TYR156 |
E | ALA157 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FES F 1917 |
Chain | Residue |
D | MET191 |
F | GLN99 |
F | CYS100 |
F | GLY101 |
F | CYS103 |
F | CYS135 |
F | ARG136 |
F | CYS137 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FES F 1918 |
Chain | Residue |
F | GLN39 |
F | GLY40 |
F | CYS41 |
F | GLY44 |
F | GLU45 |
F | CYS46 |
F | GLY47 |
F | CYS49 |
F | CYS61 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EPE A 1111 |
Chain | Residue |
A | HIS453 |
A | TRP454 |
A | THR455 |
A | GLY456 |
A | HIS459 |
A | GLN605 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGFGARTEaLhfeiiagl..........LARK |
Chain | Residue | Details |
A | LEU241-LYS264 |
site_id | PS00197 |
Number of Residues | 9 |
Details | 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CDGGECGAC |
Chain | Residue | Details |
C | CYS41-CYS49 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
C | CYS41 | |
F | CYS46 | |
F | CYS49 | |
F | CYS61 | |
F | CYS100 | |
F | CYS103 | |
F | CYS135 | |
F | CYS137 | |
C | CYS46 | |
C | CYS49 | |
C | CYS61 | |
C | CYS100 | |
C | CYS103 | |
C | CYS135 | |
C | CYS137 | |
F | CYS41 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
B | CYS122 | |
B | CYS138 | |
B | CYS146 | |
B | CYS155 | |
E | CYS122 | |
E | CYS138 | |
E | CYS146 | |
E | CYS155 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
A | GLU723 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
D | GLU723 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
A | GLN214 | |
A | ARG358 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
D | GLN214 | |
D | ARG358 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
A | GLU726 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
D | GLU726 |