7MGY
Sco GlgEI-V279S in complex with 4-alpha-glucoside of valienamine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0004556 | molecular_function | alpha-amylase activity |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0009313 | biological_process | oligosaccharide catabolic process |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0016758 | molecular_function | hexosyltransferase activity |
A | 0030979 | biological_process | alpha-glucan biosynthetic process |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0004556 | molecular_function | alpha-amylase activity |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0009313 | biological_process | oligosaccharide catabolic process |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0016758 | molecular_function | hexosyltransferase activity |
B | 0030979 | biological_process | alpha-glucan biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue ZD1 A 701 |
Chain | Residue |
A | LYS264 |
A | ASN395 |
A | GLU423 |
A | ASP480 |
A | LYS534 |
A | TYR535 |
A | HOH811 |
A | HOH1222 |
A | HOH1246 |
A | ASN268 |
A | SER279 |
A | TRP281 |
A | ALA282 |
A | GLN324 |
A | TYR357 |
A | ASP359 |
A | ASP394 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue PGE A 702 |
Chain | Residue |
A | THR426 |
A | TYR445 |
A | TRP448 |
A | HOH999 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue PGE A 703 |
Chain | Residue |
A | ARG66 |
A | GLU105 |
A | ARG191 |
A | HOH1061 |
A | HOH1198 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue PEG A 704 |
Chain | Residue |
A | GLN592 |
A | GLY593 |
site_id | AC5 |
Number of Residues | 16 |
Details | binding site for residue ZD1 B 701 |
Chain | Residue |
B | LYS264 |
B | ASN268 |
B | SER279 |
B | TRP281 |
B | ALA282 |
B | GLN324 |
B | TYR357 |
B | ASP359 |
B | ASP394 |
B | ASN395 |
B | GLU423 |
B | ASP480 |
B | LYS534 |
B | TYR535 |
B | HOH822 |
B | HOH1072 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue PGE B 702 |
Chain | Residue |
B | GLN592 |
B | GLY593 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue PGE B 703 |
Chain | Residue |
B | TRP448 |
B | HOH994 |
Functional Information from PROSITE/UniProt
site_id | PS00430 |
Number of Residues | 50 |
Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mpathhssatsaerptvvgripvldvrpvvqrgrrpakavtg.........................................................................ESFEVSAT |
Chain | Residue | Details |
A | MET1-THR50 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:21914799 |
Chain | Residue | Details |
B | ASP394 | |
A | ASP394 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:21914799 |
Chain | Residue | Details |
B | GLU423 | |
A | GLU423 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000305|PubMed:21914799 |
Chain | Residue | Details |
B | ASN395 | |
B | LYS534 | |
A | LYS534 | |
B | LYS264 | |
B | GLN324 | |
B | ASP359 | |
A | LYS264 | |
A | GLN324 | |
A | ASP359 | |
A | ASN395 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:21914799 |
Chain | Residue | Details |
B | ASP480 | |
A | ASP480 |