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 | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"31316802","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"31316802","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31316802","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
