5OI0
Crystal structure of Mycolicibacterium hassiacum glucosylglycerate hydrolase (MhGgH) 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 | 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 | 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 | 5 |
Details | binding site for residue GOL A 501 |
Chain | Residue |
A | GLY150 |
A | MET153 |
A | ARG154 |
A | ARG157 |
A | ASP279 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
B | GLN11 |
B | ARG125 |
B | HIS129 |
B | GLY446 |
A | GLU399 |
A | ARG402 |
A | HOH626 |
A | HOH672 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | GLN11 |
A | ARG125 |
A | HIS129 |
A | GLY446 |
A | HOH622 |
A | HOH628 |
A | HOH836 |
B | GLU399 |
B | ARG402 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | TYR36 |
A | TRP40 |
A | TRP42 |
A | ASP43 |
A | GLN115 |
A | TYR375 |
A | GLN434 |
A | SER510 |
A | HOH702 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL A 505 |
Chain | Residue |
A | LEU25 |
A | GLY26 |
A | THR27 |
A | ALA82 |
A | ASN83 |
A | ARG108 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue GOL A 506 |
Chain | Residue |
A | HIS334 |
B | GLN264 |
B | TYR284 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue GOL A 507 |
Chain | Residue |
B | HIS334 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue GOL A 508 |
Chain | Residue |
A | GLU296 |
A | THR297 |
A | THR298 |
A | ARG306 |
A | TRP315 |
A | HOH801 |
A | HOH883 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue GOL A 509 |
Chain | Residue |
A | TYR202 |
A | GLN203 |
A | ARG204 |
A | ASP219 |
A | ASP223 |
site_id | AD1 |
Number of Residues | 11 |
Details | binding site for residue SER A 510 |
Chain | Residue |
A | TRP40 |
A | HIS78 |
A | TYR88 |
A | TRP177 |
A | ASP182 |
A | ARG216 |
A | TYR222 |
A | TYR375 |
A | GOL504 |
A | HOH636 |
A | HOH658 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue GOL B 501 |
Chain | Residue |
B | MET153 |
B | ARG154 |
B | ARG157 |
B | ASP279 |
B | HOH819 |
site_id | AD3 |
Number of Residues | 9 |
Details | binding site for residue GOL B 502 |
Chain | Residue |
B | TYR36 |
B | TRP40 |
B | TRP42 |
B | ASP43 |
B | GLN115 |
B | TYR375 |
B | GLN434 |
B | SER505 |
B | HOH647 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue GOL B 503 |
Chain | Residue |
B | LEU25 |
B | GLY26 |
B | THR27 |
B | ASN83 |
B | ARG108 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue GOL B 504 |
Chain | Residue |
B | GLU296 |
B | THR297 |
B | THR298 |
B | GLN300 |
B | ARG306 |
B | TRP315 |
site_id | AD6 |
Number of Residues | 12 |
Details | binding site for residue SER B 505 |
Chain | Residue |
B | HOH650 |
B | HOH663 |
B | TYR36 |
B | TRP40 |
B | HIS78 |
B | TYR88 |
B | TRP177 |
B | ASP182 |
B | ARG216 |
B | TYR222 |
B | TYR375 |
B | GOL502 |
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 |