4STD
HIGH RESOLUTION STRUCTURES OF SCYTALONE DEHYDRATASE-INHIBITOR COMPLEXES CRYSTALLIZED AT PHYSIOLOGICAL PH
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005575 | cellular_component | cellular_component |
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 | 0005575 | cellular_component | cellular_component |
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 | 0005575 | cellular_component | cellular_component |
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 | 17 |
Details | BINDING SITE FOR RESIDUE BFS A 173 |
Chain | Residue |
A | TYR30 |
A | LEU147 |
A | PRO149 |
A | ILE151 |
A | PHE158 |
A | PHE162 |
A | GLY165 |
A | HOH187 |
A | HOH190 |
A | TYR50 |
A | VAL75 |
A | LEU76 |
A | LEU106 |
A | HIS110 |
A | ALA127 |
A | SER129 |
A | ASN131 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE BFS B 174 |
Chain | Residue |
B | TYR30 |
B | TYR50 |
B | VAL108 |
B | HIS110 |
B | ALA127 |
B | SER129 |
B | ASN131 |
B | LEU147 |
B | PRO149 |
B | PHE158 |
B | PHE162 |
B | HOH189 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE BFS C 175 |
Chain | Residue |
C | TYR30 |
C | TYR50 |
C | PHE53 |
C | LEU76 |
C | LEU106 |
C | VAL108 |
C | HIS110 |
C | ALA127 |
C | SER129 |
C | ASN131 |
C | LEU147 |
C | PHE158 |
C | GLY165 |
C | HOH185 |
C | HOH188 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:7866745 |
Chain | Residue | Details |
A | HIS85 | |
A | HIS110 | |
B | HIS85 | |
B | HIS110 | |
C | HIS85 | |
C | HIS110 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:9922139 |
Chain | Residue | Details |
A | TYR30 | |
B | TYR30 | |
C | TYR30 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:9665698 |
Chain | Residue | Details |
A | TYR50 | |
B | TYR50 | |
C | TYR50 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:10382670 |
Chain | Residue | Details |
A | PHE53 | |
B | PHE53 | |
C | PHE53 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:10382670, ECO:0000305|PubMed:7866745, ECO:0000305|PubMed:9922139 |
Chain | Residue | Details |
A | ASN131 | |
B | ASN131 | |
C | ASN131 |
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 |