7STD
SCYTALONE DEHYDRATASE PLUS INHIBITOR 4
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005768 | cellular_component | endosome |
| A | 0006582 | biological_process | melanin metabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030411 | molecular_function | scytalone dehydratase activity |
| A | 0042438 | biological_process | melanin biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005768 | cellular_component | endosome |
| B | 0006582 | biological_process | melanin metabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0030411 | molecular_function | scytalone dehydratase activity |
| B | 0042438 | biological_process | melanin biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005768 | cellular_component | endosome |
| C | 0006582 | biological_process | melanin metabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0030411 | molecular_function | scytalone dehydratase activity |
| C | 0042438 | biological_process | melanin biosynthetic process |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 501 |
| Chain | Residue |
| A | GLU163 |
| A | GLU163 |
| A | ASP164 |
| A | ASP164 |
| A | GLU167 |
| A | GLU167 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 501 |
| Chain | Residue |
| B | HOH683 |
| B | ARG51 |
| B | ASP55 |
| B | GLU59 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 502 |
| Chain | Residue |
| B | ASP171 |
| B | HOH645 |
| B | HOH656 |
| B | HOH680 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 501 |
| Chain | Residue |
| C | ARG51 |
| C | ASP55 |
| C | GLU59 |
| C | HOH669 |
| C | HOH709 |
| C | HOH744 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA C 502 |
| Chain | Residue |
| C | ASP171 |
| C | HOH634 |
| C | HOH648 |
| C | HOH650 |
| C | HOH664 |
| C | HOH708 |
| C | HOH743 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CRP A 600 |
| Chain | Residue |
| A | TYR50 |
| A | PHE53 |
| A | VAL75 |
| A | LEU76 |
| A | VAL108 |
| A | ASN131 |
| A | PRO149 |
| A | ILE151 |
| A | GLY165 |
| A | HOH628 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CRP B 601 |
| Chain | Residue |
| B | TRP26 |
| B | TYR50 |
| B | PHE53 |
| B | VAL75 |
| B | VAL108 |
| B | ASN131 |
| B | PRO149 |
| B | ILE151 |
| B | GLY165 |
| B | HOH610 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CRP C 602 |
| Chain | Residue |
| C | TRP26 |
| C | TYR50 |
| C | PHE53 |
| C | LEU76 |
| C | VAL108 |
| C | ASN131 |
| C | GLY165 |
| C | HOH613 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"7866745","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9922139","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9665698","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10382670","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10382670","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"7866745","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9922139","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1std |
| Chain | Residue | Details |
| A | HIS85 | |
| A | ASP31 | |
| A | TYR30 | |
| A | HIS110 | |
| A | TYR50 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1std |
| Chain | Residue | Details |
| B | HIS85 | |
| B | ASP31 | |
| B | TYR30 | |
| B | HIS110 | |
| B | TYR50 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1std |
| Chain | Residue | Details |
| C | HIS85 | |
| C | ASP31 | |
| C | TYR30 | |
| C | HIS110 | |
| C | TYR50 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 910 |
| Chain | Residue | Details |
| A | TYR30 | modifies pKa |
| A | ASP31 | modifies pKa |
| A | TYR50 | proton acceptor, proton donor |
| A | HIS85 | proton acceptor, proton donor |
| A | HIS110 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 910 |
| Chain | Residue | Details |
| B | TYR30 | modifies pKa |
| B | ASP31 | modifies pKa |
| B | TYR50 | proton acceptor, proton donor |
| B | HIS85 | proton acceptor, proton donor |
| B | HIS110 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 910 |
| Chain | Residue | Details |
| C | TYR30 | modifies pKa |
| C | ASP31 | modifies pKa |
| C | TYR50 | proton acceptor, proton donor |
| C | HIS85 | proton acceptor, proton donor |
| C | HIS110 | electrostatic stabiliser |
