1DAM
DETHIOBIOTIN SYNTHETASE COMPLEXED WITH DETHIOBIOTIN, ADP, INORGANIC PHOSPHATE AND MAGNESIUM
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004141 | molecular_function | dethiobiotin synthase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0009102 | biological_process | biotin biosynthetic process |
A | 0016874 | molecular_function | ligase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG A 901 |
Chain | Residue |
A | THR16 |
A | ASP54 |
A | GLU115 |
A | HOH444 |
A | ADP801 |
A | PO4802 |
A | MG902 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG A 902 |
Chain | Residue |
A | HOH749 |
A | HOH750 |
A | ADP801 |
A | PO4802 |
A | MG901 |
A | HOH444 |
A | HOH448 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PO4 A 802 |
Chain | Residue |
A | THR11 |
A | LYS15 |
A | LYS37 |
A | ASP54 |
A | GLU115 |
A | ALA117 |
A | GLY118 |
A | HOH719 |
A | HOH749 |
A | ADP801 |
A | DTB803 |
A | MG901 |
A | MG902 |
site_id | AC4 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ADP A 801 |
Chain | Residue |
A | GLU12 |
A | VAL13 |
A | GLY14 |
A | LYS15 |
A | THR16 |
A | VAL17 |
A | GLU115 |
A | ASN175 |
A | ASP176 |
A | PRO204 |
A | TRP205 |
A | LEU206 |
A | PRO210 |
A | GLU211 |
A | HOH444 |
A | HOH448 |
A | HOH714 |
A | HOH759 |
A | PO4802 |
A | MG901 |
A | MG902 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE DTB A 803 |
Chain | Residue |
A | THR11 |
A | SER41 |
A | SER81 |
A | LEU149 |
A | GLY150 |
A | CYS151 |
A | ILE152 |
A | ASN153 |
A | TYR187 |
A | HOH655 |
A | HOH717 |
A | HOH749 |
A | PO4802 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00336, ECO:0000305|PubMed:9125495 |
Chain | Residue | Details |
A | PRO38 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9865950, ECO:0007744|PDB:1BS1 |
Chain | Residue | Details |
A | VAL13 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00336, ECO:0000269|PubMed:9576910, ECO:0000269|PubMed:9865950, ECO:0007744|PDB:1A82, ECO:0007744|PDB:1BS1, ECO:0007744|PDB:1DAK, ECO:0007744|PDB:1DAM |
Chain | Residue | Details |
A | VAL17 | |
A | ALA55 | |
A | GLY116 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00336, ECO:0000269|PubMed:7669756, ECO:0000269|PubMed:9576910, ECO:0000269|PubMed:9865950, ECO:0007744|PDB:1BS1, ECO:0007744|PDB:1DAE, ECO:0007744|PDB:1DAF, ECO:0007744|PDB:1DAG, ECO:0007744|PDB:1DAH, ECO:0007744|PDB:1DAI, ECO:0007744|PDB:1DAK, ECO:0007744|PDB:1DAM |
Chain | Residue | Details |
A | GLY42 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00336, ECO:0000269|PubMed:7669756, ECO:0000269|PubMed:9576910, ECO:0000269|PubMed:9865950, ECO:0007744|PDB:1A82, ECO:0007744|PDB:1BS1, ECO:0007744|PDB:1DAD, ECO:0007744|PDB:1DAF, ECO:0007744|PDB:1DAG, ECO:0007744|PDB:1DAH, ECO:0007744|PDB:1DAK, ECO:0007744|PDB:1DAM |
Chain | Residue | Details |
A | ASP176 | |
A | TRP205 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7669756, ECO:0000269|PubMed:9576910, ECO:0000269|PubMed:9865950, ECO:0007744|PDB:1A82, ECO:0007744|PDB:1BS1, ECO:0007744|PDB:1DAE, ECO:0007744|PDB:1DAF, ECO:0007744|PDB:1DAG, ECO:0007744|PDB:1DAH, ECO:0007744|PDB:1DAI, ECO:0007744|PDB:1DAK, ECO:0007744|PDB:1DAM |
Chain | Residue | Details |
A | MET188 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00336, ECO:0000269|PubMed:7669756, ECO:0000269|PubMed:9576910, ECO:0000269|PubMed:9865950, ECO:0007744|PDB:1A82, ECO:0007744|PDB:1BS1, ECO:0007744|PDB:1DAD, ECO:0007744|PDB:1DAF, ECO:0007744|PDB:1DAH, ECO:0007744|PDB:1DAK, ECO:0007744|PDB:1DAM |
Chain | Residue | Details |
A | ASN212 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1dak |
Chain | Residue | Details |
A | LYS15 | |
A | LYS37 | |
A | THR11 | |
A | SER41 |
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 74 |
Chain | Residue | Details |
A | GLU12 | electrostatic stabiliser |
A | VAL13 | metal ligand |
A | THR16 | electrostatic stabiliser, hydrogen bond donor |
A | VAL17 | metal ligand |
A | PRO38 | electrostatic stabiliser, hydrogen bond donor |
A | GLY42 | electrostatic stabiliser, hydrogen bond donor |
A | ALA55 | metal ligand |
A | GLY116 | metal ligand |