4EEC
Crystal Structure of the glycopeptide antibiotic sulfotransferase StaL complexed with A3P and desulfo-A47934.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008146 | molecular_function | sulfotransferase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0017000 | biological_process | antibiotic biosynthetic process |
B | 0008146 | molecular_function | sulfotransferase activity |
B | 0016740 | molecular_function | transferase activity |
B | 0017000 | biological_process | antibiotic biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE 0UZ C 405 |
Chain | Residue |
A | LYS103 |
A | ARG130 |
C | GHP404 |
C | OMY406 |
C | 3FG407 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE A3P A 301 |
Chain | Residue |
A | HIS16 |
A | TRP17 |
A | ARG90 |
A | SER98 |
A | ARG101 |
A | TYR163 |
A | CYS196 |
A | THR197 |
A | LEU198 |
A | MET201 |
A | LYS12 |
A | ALA13 |
A | GLY14 |
A | GLY15 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P49891","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"17329243","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17329243","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22753479","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"22753479","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |