1WVE
p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004458 | molecular_function | D-lactate dehydrogenase (cytochrome) activity |
| A | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018695 | molecular_function | 4-cresol dehydrogenase (hydroxylating) activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0071949 | molecular_function | FAD binding |
| A | 1903457 | biological_process | lactate catabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004458 | molecular_function | D-lactate dehydrogenase (cytochrome) activity |
| B | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0018695 | molecular_function | 4-cresol dehydrogenase (hydroxylating) activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0071949 | molecular_function | FAD binding |
| B | 1903457 | biological_process | lactate catabolic process |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1703 |
| Chain | Residue |
| B | MET48 |
| B | GLY94 |
| B | GLY96 |
| B | SER97 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 2703 |
| Chain | Residue |
| A | MET48 |
| A | GLY94 |
| A | GLY96 |
| A | SER97 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD A 599 |
| Chain | Residue |
| A | THR86 |
| A | SER88 |
| A | THR89 |
| A | GLY90 |
| A | ARG91 |
| A | ASN92 |
| A | PHE93 |
| A | SER153 |
| A | ALA154 |
| A | PRO155 |
| A | ALA159 |
| A | GLY160 |
| A | GLY163 |
| A | ASN164 |
| A | MET166 |
| A | GLY169 |
| A | VAL170 |
| A | TYR172 |
| A | CYS231 |
| A | GLU380 |
| A | TYR384 |
| A | TRP394 |
| A | ARG474 |
| A | ARG512 |
| A | ACY1701 |
| A | HOH2717 |
| A | HOH2718 |
| A | HOH2735 |
| A | HOH2749 |
| A | HOH3184 |
| A | HOH3190 |
| A | TRP85 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS A 1704 |
| Chain | Residue |
| A | ARG415 |
| A | GLU460 |
| A | GLU464 |
| A | LYS467 |
| A | TRS2705 |
| A | HOH2973 |
| A | HOH3016 |
| D | PHE647 |
| D | HEM699 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE TRS B 1705 |
| Chain | Residue |
| B | GLN102 |
| B | ASP481 |
| B | TRS2704 |
| B | HOH2724 |
| B | HOH2766 |
| B | HOH2935 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM C 699 |
| Chain | Residue |
| A | PHE381 |
| B | LYS419 |
| C | VAL614 |
| C | CYS615 |
| C | CYS618 |
| C | HIS619 |
| C | VAL625 |
| C | GLY626 |
| C | PRO627 |
| C | LEU629 |
| C | TYR638 |
| C | ILE639 |
| C | ILE642 |
| C | VAL643 |
| C | PHE647 |
| C | ARG648 |
| C | ALA649 |
| C | MET650 |
| C | HOH718 |
| C | HOH719 |
| C | HOH777 |
| C | HOH778 |
| C | HOH779 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD B 599 |
| Chain | Residue |
| B | PHE381 |
| B | TYR384 |
| B | TRP394 |
| B | ARG474 |
| B | ARG512 |
| B | ACY1702 |
| B | HOH2709 |
| B | HOH2710 |
| B | HOH2716 |
| B | HOH2778 |
| B | HOH3130 |
| B | TRP85 |
| B | THR86 |
| B | SER88 |
| B | THR89 |
| B | GLY90 |
| B | ARG91 |
| B | ASN92 |
| B | PHE93 |
| B | SER153 |
| B | ALA154 |
| B | PRO155 |
| B | ALA159 |
| B | GLY160 |
| B | GLY163 |
| B | ASN164 |
| B | MET166 |
| B | GLY169 |
| B | VAL170 |
| B | TYR172 |
| B | CYS231 |
| B | GLU380 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TRS B 2704 |
| Chain | Residue |
| B | HIS56 |
| B | VAL101 |
| B | ARG478 |
| B | TRS1705 |
| B | HOH2805 |
| B | HOH2943 |
| B | HOH3028 |
| B | HOH3064 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TRS A 2705 |
| Chain | Residue |
| A | LYS419 |
| A | TYR420 |
| A | GLU460 |
| A | ASP463 |
| A | TRS1704 |
| A | HOH2776 |
| D | HEM699 |
| D | HOH760 |
| site_id | BC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM D 699 |
| Chain | Residue |
| A | LYS419 |
| A | TRS1704 |
| A | TRS2705 |
| B | PHE381 |
| D | VAL614 |
| D | CYS615 |
| D | CYS618 |
| D | HIS619 |
| D | VAL625 |
| D | PRO627 |
| D | LEU629 |
| D | TYR638 |
| D | ILE642 |
| D | VAL643 |
| D | PHE647 |
| D | ARG648 |
| D | MET650 |
| D | HOH716 |
| D | HOH732 |
| D | HOH770 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACY A 1701 |
| Chain | Residue |
| A | TYR95 |
| A | TRP394 |
| A | ILE429 |
| A | VAL438 |
| A | TYR473 |
| A | ARG474 |
| A | FAD599 |
| A | HOH3184 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY B 1702 |
| Chain | Residue |
| B | TYR95 |
| B | TRP394 |
| B | TYR473 |
| B | FAD599 |
| B | HOH3130 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACY A 2701 |
| Chain | Residue |
| A | GLN333 |
| A | ASN337 |
| A | HOH2896 |
| A | HOH2980 |
| A | HOH3201 |
| A | HOH3202 |
| B | ASN337 |
| site_id | BC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACY A 2702 |
| Chain | Residue |
| A | HOH2861 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 428 |
| Details | Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00718","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"O-8alpha-FAD tyrosine"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"covalent"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dii |
| Chain | Residue | Details |
| A | TYR473 | |
| A | TYR95 | |
| A | ARG474 | |
| A | GLU380 | |
| A | GLU427 | |
| A | HIS436 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dii |
| Chain | Residue | Details |
| B | TYR473 | |
| B | TYR95 | |
| B | ARG474 | |
| B | GLU380 | |
| B | GLU427 | |
| B | HIS436 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 141 |
| Chain | Residue | Details |
| B | PRO50 | polar interaction, polar/non-polar interaction, single electron acceptor, single electron donor, single electron relay |
| A | ARG512 | activator, hydrogen bond donor |
| B | VAL51 | metal ligand, polar interaction, single electron acceptor, single electron donor, single electron relay |
| A | GLU286 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | TYR367 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | GLU380 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | TYR384 | covalently attached, polar/non-polar interaction, single electron acceptor, single electron donor, single electron relay |
| A | HIS436 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | TYR473 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | ARG474 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 141 |
| Chain | Residue | Details |
| D | ALA649 | polar interaction, polar/non-polar interaction, single electron acceptor, single electron donor, single electron relay |
| D | MET650 | metal ligand, polar interaction, single electron acceptor, single electron donor, single electron relay |
