5OIV
Crystal structure of Mycolicibacterium hassiacum glucosylglycerate hydrolase (MhGgH) D43A variant in complex with serine and glycerol
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004573 | molecular_function | Glc3Man9GlcNAc2 oligosaccharide glucosidase activity |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006487 | biological_process | protein N-linked glycosylation |
A | 0008152 | biological_process | metabolic process |
A | 0009311 | biological_process | oligosaccharide metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0102547 | molecular_function | glucosylglycerate hydrolase activity |
B | 0004573 | molecular_function | Glc3Man9GlcNAc2 oligosaccharide glucosidase activity |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0006487 | biological_process | protein N-linked glycosylation |
B | 0008152 | biological_process | metabolic process |
B | 0009311 | biological_process | oligosaccharide metabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0102547 | molecular_function | glucosylglycerate hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue GOL A 501 |
Chain | Residue |
A | GLN11 |
A | ARG125 |
A | HIS129 |
A | GLY446 |
A | HOH654 |
A | HOH664 |
A | HOH754 |
B | GLU399 |
B | ARG402 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
A | GLU399 |
A | ARG402 |
A | HOH626 |
A | HOH638 |
A | HOH872 |
B | GLN11 |
B | ARG125 |
B | HIS129 |
B | GLY446 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | MET153 |
A | ARG154 |
A | ARG157 |
A | ASP279 |
A | HOH738 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | TYR36 |
A | TRP40 |
A | TRP42 |
A | GLN115 |
A | GLN434 |
A | SER510 |
A | HOH639 |
A | HOH671 |
A | HOH690 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue GOL A 505 |
Chain | Residue |
A | HIS334 |
A | HOH835 |
B | GLN264 |
B | TYR284 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue GOL A 506 |
Chain | Residue |
A | GLN264 |
A | TYR284 |
B | HIS334 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue GOL A 507 |
Chain | Residue |
A | ILE210 |
A | GLY430 |
A | MET432 |
A | HOH710 |
A | HOH825 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue GOL A 508 |
Chain | Residue |
A | TYR202 |
A | GLN203 |
A | ARG204 |
A | ASP223 |
A | HOH687 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue GOL A 509 |
Chain | Residue |
A | GLU296 |
A | THR297 |
A | THR298 |
A | TRP315 |
A | HOH614 |
site_id | AD1 |
Number of Residues | 10 |
Details | binding site for residue SER A 510 |
Chain | Residue |
A | TRP40 |
A | HIS78 |
A | TYR88 |
A | ASP182 |
A | ARG216 |
A | TYR222 |
A | TYR375 |
A | GOL504 |
A | HOH630 |
A | HOH667 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue GLY A 511 |
Chain | Residue |
A | GLU345 |
A | ARG400 |
A | LEU403 |
A | HOH635 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue GLY A 512 |
Chain | Residue |
A | ARG338 |
A | GLU345 |
A | ARG400 |
B | ASP272 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue GLY A 513 |
Chain | Residue |
A | ARG168 |
A | PHE308 |
A | TRP315 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue GOL B 501 |
Chain | Residue |
B | ARG154 |
B | ARG157 |
B | ASP279 |
B | HOH833 |
site_id | AD6 |
Number of Residues | 9 |
Details | binding site for residue GOL B 502 |
Chain | Residue |
B | TYR36 |
B | TRP40 |
B | TRP42 |
B | GLN115 |
B | GLN434 |
B | SER504 |
B | HOH616 |
B | HOH694 |
B | HOH727 |
site_id | AD7 |
Number of Residues | 7 |
Details | binding site for residue GOL B 503 |
Chain | Residue |
B | GLU296 |
B | THR297 |
B | THR298 |
B | GLN300 |
B | ARG306 |
B | TRP315 |
B | HOH728 |
site_id | AD8 |
Number of Residues | 9 |
Details | binding site for residue SER B 504 |
Chain | Residue |
B | ARG216 |
B | TYR375 |
B | GOL502 |
B | HOH617 |
B | HOH708 |
B | TRP40 |
B | HIS78 |
B | TYR88 |
B | ASP182 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:31316802 |
Chain | Residue | Details |
A | ASP182 | |
B | ASP182 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:31316802 |
Chain | Residue | Details |
A | GLU419 | |
B | GLU419 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:31316802 |
Chain | Residue | Details |
A | TYR36 | |
B | TRP40 | |
B | TYR88 | |
B | GLN115 | |
B | GLY180 | |
B | ARG216 | |
B | TYR375 | |
B | GLN434 | |
A | TRP40 | |
A | TYR88 | |
A | GLN115 | |
A | GLY180 | |
A | ARG216 | |
A | TYR375 | |
A | GLN434 | |
B | TYR36 |