1EXC
CRYSTAL STRUCTURE OF B. SUBTILIS MAF PROTEIN COMPLEXED WITH D-(UTP)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0009117 | biological_process | nucleotide metabolic process |
A | 0016462 | molecular_function | pyrophosphatase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0036218 | molecular_function | dTTP diphosphatase activity |
A | 0036221 | molecular_function | UTP diphosphatase activity |
A | 0047429 | molecular_function | nucleoside triphosphate diphosphatase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0009117 | biological_process | nucleotide metabolic process |
B | 0016462 | molecular_function | pyrophosphatase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0036218 | molecular_function | dTTP diphosphatase activity |
B | 0036221 | molecular_function | UTP diphosphatase activity |
B | 0047429 | molecular_function | nucleoside triphosphate diphosphatase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA A 205 |
Chain | Residue |
A | GLU116 |
A | HIS184 |
B | GLU116 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DUT A 201 |
Chain | Residue |
A | HOH209 |
A | HOH273 |
A | SER9 |
A | GLN10 |
A | ARG14 |
A | GLU34 |
A | LYS53 |
A | LYS82 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE DUT B 202 |
Chain | Residue |
B | SER9 |
B | GLN10 |
B | SER11 |
B | ARG14 |
B | SER30 |
B | VAL32 |
B | GLU34 |
B | LYS53 |
B | ALA69 |
B | LYS82 |
B | HOH274 |
B | HOH311 |
B | HOH338 |
B | HOH344 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DUT B 203 |
Chain | Residue |
A | DUT204 |
B | PHE40 |
B | GLU44 |
B | TRP48 |
B | HOH327 |
B | HOH333 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE DUT A 204 |
Chain | Residue |
A | TRP48 |
A | LYS51 |
A | LYS55 |
A | HOH307 |
A | HOH331 |
B | LYS51 |
B | LYS55 |
B | DUT203 |
B | HOH327 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000305|PubMed:24210219 |
Chain | Residue | Details |
A | ASP70 | |
B | ASP70 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | SITE: Important for substrate specificity => ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000305|PubMed:24210219 |
Chain | Residue | Details |
A | ARG13 | |
A | THR71 | |
A | GLN153 | |
B | ARG13 | |
B | THR71 | |
B | GLN153 |