1DII
CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE AT 2.5 A RESOLUTION
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 A 701 |
| Chain | Residue |
| A | MET48 |
| A | GLY94 |
| A | GLY96 |
| A | SER97 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 702 |
| Chain | Residue |
| B | MET48 |
| B | GLY94 |
| B | GLY96 |
| B | SER97 |
| site_id | AC3 |
| Number of Residues | 30 |
| 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 | PRO155 |
| A | ALA159 |
| A | GLY160 |
| A | GLY163 |
| A | ASN164 |
| A | MET166 |
| A | GLY169 |
| A | VAL170 |
| A | TYR172 |
| A | GLY229 |
| A | ILE230 |
| A | CYS231 |
| A | GLU380 |
| A | TYR384 |
| A | TRP394 |
| A | ARG474 |
| A | ARG512 |
| A | HOH729 |
| A | HOH757 |
| A | HOH786 |
| A | HOH846 |
| A | TRP85 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC C 699 |
| Chain | Residue |
| A | PHE381 |
| B | LYS419 |
| C | HOH47 |
| C | VAL614 |
| C | CYS615 |
| C | CYS618 |
| C | HIS619 |
| C | VAL625 |
| C | PRO627 |
| C | LEU629 |
| C | ARG632 |
| C | TYR638 |
| C | ILE639 |
| C | ILE642 |
| C | VAL643 |
| C | PHE647 |
| C | ARG648 |
| C | ALA649 |
| C | MET650 |
| site_id | AC5 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD B 599 |
| Chain | Residue |
| 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 |
| B | TYR384 |
| B | TRP394 |
| B | ARG474 |
| B | ARG512 |
| B | HOH731 |
| B | HOH814 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEC D 699 |
| Chain | Residue |
| D | ARG648 |
| D | ALA649 |
| D | MET650 |
| A | LYS419 |
| B | PHE381 |
| D | HOH302 |
| D | HOH366 |
| D | VAL614 |
| D | CYS615 |
| D | CYS618 |
| D | HIS619 |
| D | VAL625 |
| D | ARG632 |
| D | TYR638 |
| D | ILE639 |
| D | ILE642 |
| D | VAL643 |
| D | PHE647 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: covalent |
| Chain | Residue | Details |
| C | CYS615 | |
| C | CYS618 | |
| D | CYS615 | |
| D | CYS618 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| C | HIS619 | |
| C | MET650 | |
| D | HIS619 | |
| D | MET650 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 10623531 |
| Chain | Residue | Details |
| A | TYR473 | |
| A | GLU380 | |
| A | HIS436 | |
| A | ARG474 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 141 |
| Chain | Residue | Details |
| B | MET49 | polar interaction, polar/non-polar interaction, single electron acceptor, single electron donor, single electron relay |
| A | ARG512 | activator, hydrogen bond donor |
| B | PRO50 | 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 |
