6IYL
The structure of EntE with 3-cyanobenzoyl adenylate analog
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0008668 | molecular_function | 2,3-dihydroxybenzoate--[aryl-carrier protein] ligase |
A | 0009239 | biological_process | enterobactin biosynthetic process |
A | 0016020 | cellular_component | membrane |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0016874 | molecular_function | ligase activity |
A | 0016877 | molecular_function | ligase activity, forming carbon-sulfur bonds |
A | 0019290 | biological_process | siderophore biosynthetic process |
A | 0047527 | molecular_function | 2,3-dihydroxybenzoate-serine ligase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005829 | cellular_component | cytosol |
B | 0008668 | molecular_function | 2,3-dihydroxybenzoate--[aryl-carrier protein] ligase |
B | 0009239 | biological_process | enterobactin biosynthetic process |
B | 0016020 | cellular_component | membrane |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0016874 | molecular_function | ligase activity |
B | 0016877 | molecular_function | ligase activity, forming carbon-sulfur bonds |
B | 0019290 | biological_process | siderophore biosynthetic process |
B | 0047527 | molecular_function | 2,3-dihydroxybenzoate-serine ligase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | binding site for residue B1X A 601 |
Chain | Residue |
A | HIS234 |
A | MET334 |
A | ALA335 |
A | ASP415 |
A | LYS432 |
A | LYS441 |
A | HOH715 |
A | HOH719 |
A | HOH739 |
A | HOH751 |
A | TYR236 |
A | SER240 |
A | GLY309 |
A | ALA310 |
A | ARG311 |
A | VAL331 |
A | PHE332 |
A | GLY333 |
site_id | AC2 |
Number of Residues | 17 |
Details | binding site for residue B1X B 601 |
Chain | Residue |
B | HIS234 |
B | GLY235 |
B | TYR236 |
B | SER239 |
B | SER240 |
B | GLY309 |
B | ALA310 |
B | ARG311 |
B | VAL331 |
B | PHE332 |
B | GLY333 |
B | MET334 |
B | ALA335 |
B | GLN355 |
B | ASP415 |
B | LYS432 |
B | LYS441 |
Functional Information from PROSITE/UniProt
site_id | PS00455 |
Number of Residues | 12 |
Details | AMP_BINDING Putative AMP-binding domain signature. FQLSGGTTGtPK |
Chain | Residue | Details |
A | PHE187-LYS198 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22365602 |
Chain | Residue | Details |
A | GLY235 | |
A | ALA335 | |
B | GLY235 | |
B | ALA335 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23897471 |
Chain | Residue | Details |
A | SER240 | |
A | LYS432 | |
A | LYS441 | |
B | SER240 | |
B | LYS432 | |
B | LYS441 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22365602, ECO:0000269|PubMed:23897471 |
Chain | Residue | Details |
A | GLY309 | |
A | VAL331 | |
A | ASP415 | |
B | GLY309 | |
B | VAL331 | |
B | ASP415 |