5OHZ
Crystal structure of Mycolicibacterium hassiacum glucosylglycerate hydrolase (MhGgH) - SeMet derivative
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 |
C | 0004573 | molecular_function | Glc3Man9GlcNAc2 oligosaccharide glucosidase activity |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0006487 | biological_process | protein N-linked glycosylation |
C | 0009311 | biological_process | oligosaccharide metabolic process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
C | 0102547 | molecular_function | glucosylglycerate hydrolase activity |
D | 0004573 | molecular_function | Glc3Man9GlcNAc2 oligosaccharide glucosidase activity |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0006487 | biological_process | protein N-linked glycosylation |
D | 0009311 | biological_process | oligosaccharide metabolic process |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
D | 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 | TYR36 |
A | TRP40 |
A | TRP42 |
A | ASP43 |
A | GLN115 |
A | GLN434 |
A | TRP436 |
A | SER505 |
A | HOH615 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
A | GLU296 |
A | THR297 |
A | THR298 |
A | ARG306 |
A | TRP315 |
A | HOH702 |
A | HOH784 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | HIS334 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | TRP386 |
A | SER389 |
A | TRP390 |
A | ASP443 |
A | TRP444 |
A | HOH668 |
A | HOH697 |
A | HOH800 |
site_id | AC5 |
Number of Residues | 11 |
Details | binding site for residue SER A 505 |
Chain | Residue |
A | TRP40 |
A | HIS78 |
A | TYR88 |
A | ASP182 |
A | ARG216 |
A | TYR222 |
A | TYR375 |
A | GOL501 |
A | HOH607 |
A | HOH625 |
A | HOH643 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue GOL B 501 |
Chain | Residue |
B | TYR36 |
B | TRP40 |
B | TRP42 |
B | ASP43 |
B | GLN115 |
B | TYR375 |
B | GLN434 |
B | TRP436 |
B | SER507 |
B | HOH673 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue GOL B 502 |
Chain | Residue |
A | GLN11 |
B | ARG125 |
B | HIS129 |
B | GLY446 |
B | HOH609 |
B | HOH634 |
D | GLU399 |
D | ARG402 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue GOL B 503 |
Chain | Residue |
B | HIS334 |
D | TYR284 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue GOL B 504 |
Chain | Residue |
B | TRP149 |
B | GLY150 |
B | MSE153 |
B | PRO276 |
B | ASP279 |
B | HOH759 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue GOL B 505 |
Chain | Residue |
B | GLU296 |
B | THR297 |
B | THR298 |
B | ARG306 |
B | TRP315 |
B | HOH623 |
B | HOH685 |
B | HOH788 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue GOL B 506 |
Chain | Residue |
B | TRP386 |
B | SER389 |
B | TRP390 |
B | ASP443 |
B | TRP444 |
B | HOH664 |
B | HOH754 |
B | HOH762 |
site_id | AD3 |
Number of Residues | 11 |
Details | binding site for residue SER B 507 |
Chain | Residue |
B | TRP40 |
B | HIS78 |
B | TYR88 |
B | ASP182 |
B | ARG216 |
B | TYR222 |
B | TYR375 |
B | GOL501 |
B | HOH618 |
B | HOH652 |
B | HOH689 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue GOL C 501 |
Chain | Residue |
A | ARG125 |
A | HIS129 |
A | GLY446 |
B | GLN11 |
C | GLU399 |
C | ARG402 |
C | HOH647 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue GOL C 502 |
Chain | Residue |
C | ASP43 |
C | GLN115 |
C | GLN434 |
C | SER505 |
C | HOH627 |
C | TYR36 |
C | TRP40 |
C | TRP42 |
site_id | AD6 |
Number of Residues | 7 |
Details | binding site for residue GOL C 503 |
Chain | Residue |
A | GLU399 |
A | ARG402 |
C | ARG125 |
C | HIS129 |
C | GLY446 |
C | HOH619 |
D | GLN11 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue GOL C 504 |
Chain | Residue |
C | THR297 |
C | THR298 |
C | ASP299 |
C | ARG306 |
C | TRP315 |
C | HOH741 |
site_id | AD8 |
Number of Residues | 9 |
Details | binding site for residue SER C 505 |
Chain | Residue |
C | TYR36 |
C | TRP40 |
C | HIS78 |
C | TYR88 |
C | ASP182 |
C | ARG216 |
C | TYR375 |
C | GOL502 |
C | HOH644 |
site_id | AD9 |
Number of Residues | 9 |
Details | binding site for residue GOL D 501 |
Chain | Residue |
D | TYR36 |
D | TRP40 |
D | TRP42 |
D | ASP43 |
D | GLN115 |
D | GLN434 |
D | TRP436 |
D | SER503 |
D | HOH636 |
site_id | AE1 |
Number of Residues | 9 |
Details | binding site for residue GOL D 502 |
Chain | Residue |
B | GLU399 |
B | ARG402 |
B | HOH909 |
C | GLN11 |
D | ARG125 |
D | HIS129 |
D | ASP443 |
D | GLY446 |
D | HOH664 |
site_id | AE2 |
Number of Residues | 10 |
Details | binding site for residue SER D 503 |
Chain | Residue |
D | TRP40 |
D | HIS78 |
D | TYR88 |
D | ASP182 |
D | ARG216 |
D | TYR222 |
D | TYR375 |
D | GOL501 |
D | HOH612 |
D | HOH706 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:31316802 |
Chain | Residue | Details |
A | ASP182 | |
B | ASP182 | |
C | ASP182 | |
D | ASP182 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:31316802 |
Chain | Residue | Details |
A | GLU419 | |
B | GLU419 | |
C | GLU419 | |
D | GLU419 |
site_id | SWS_FT_FI3 |
Number of Residues | 32 |
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 | |
C | TYR36 | |
C | TRP40 | |
C | TYR88 | |
A | TRP40 | |
C | GLN115 | |
C | GLY180 | |
C | ARG216 | |
C | TYR375 | |
C | GLN434 | |
D | TYR36 | |
D | TRP40 | |
D | TYR88 | |
D | GLN115 | |
D | GLY180 | |
A | TYR88 | |
D | ARG216 | |
D | TYR375 | |
D | GLN434 | |
A | GLN115 | |
A | GLY180 | |
A | ARG216 | |
A | TYR375 | |
A | GLN434 | |
B | TYR36 |