1GQI
Structure of Pseudomonas cellulosa alpha-D-glucuronidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0005576 | cellular_component | extracellular region |
| A | 0009279 | cellular_component | cell outer membrane |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0033939 | molecular_function | xylan alpha-1,2-glucuronosidase activity |
| A | 0045493 | biological_process | xylan catabolic process |
| A | 0046559 | molecular_function | alpha-glucuronidase activity |
| A | 2000886 | biological_process | glucuronoxylan catabolic process |
| B | 0000272 | biological_process | polysaccharide catabolic process |
| B | 0005576 | cellular_component | extracellular region |
| B | 0009279 | cellular_component | cell outer membrane |
| B | 0016020 | cellular_component | membrane |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0033939 | molecular_function | xylan alpha-1,2-glucuronosidase activity |
| B | 0045493 | biological_process | xylan catabolic process |
| B | 0046559 | molecular_function | alpha-glucuronidase activity |
| B | 2000886 | biological_process | glucuronoxylan catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CO A1719 |
| Chain | Residue |
| A | THR629 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A1720 |
| Chain | Residue |
| A | GLY7 |
| A | ASN452 |
| A | PRO457 |
| A | HOH2598 |
| A | HOH2793 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CO A1721 |
| Chain | Residue |
| A | ASN607 |
| A | TRP609 |
| A | ARG673 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A1722 |
| Chain | Residue |
| A | ASN162 |
| A | ASN164 |
| A | TRP702 |
| A | HOH2889 |
| A | HOH2890 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A1723 |
| Chain | Residue |
| A | HOH2107 |
| A | HOH2266 |
| A | HOH2268 |
| A | HOH2439 |
| A | HOH2441 |
| A | HOH2544 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CO B1719 |
| Chain | Residue |
| B | THR629 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO B1720 |
| Chain | Residue |
| B | GLY7 |
| B | ASN452 |
| B | PRO457 |
| B | HOH2591 |
| B | HOH2786 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO B1721 |
| Chain | Residue |
| A | HOH2872 |
| B | ASN162 |
| B | ASN164 |
| B | TRP702 |
| B | HOH2875 |
| B | HOH2876 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CO B1722 |
| Chain | Residue |
| B | ASN607 |
| B | TRP609 |
| B | ARG673 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B1723 |
| Chain | Residue |
| B | HOH2111 |
| B | HOH2265 |
| B | HOH2266 |
| B | HOH2440 |
| B | HOH2441 |
| B | HOH2537 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A1713 |
| Chain | Residue |
| A | TYR101 |
| A | ARG133 |
| A | SER199 |
| A | LEU200 |
| A | TRP471 |
| A | EDO1715 |
| A | HOH2306 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A1714 |
| Chain | Residue |
| A | ARG51 |
| A | PRO188 |
| A | ASP192 |
| A | ARG195 |
| A | HOH2297 |
| A | HOH2883 |
| A | HOH2884 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A1715 |
| Chain | Residue |
| A | HIS130 |
| A | ARG133 |
| A | SER148 |
| A | ARG468 |
| A | TRP471 |
| A | ILE475 |
| A | EDO1713 |
| A | HOH2602 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A1716 |
| Chain | Residue |
| A | TYR8 |
| A | ASP9 |
| A | LEU12 |
| A | ASP192 |
| A | ARG195 |
| A | ILE196 |
| A | HOH2017 |
| A | HOH2027 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A1717 |
| Chain | Residue |
| A | ASP178 |
| A | TYR185 |
| A | HOH2886 |
| B | GLY455 |
| B | GLN644 |
| B | LEU648 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A1718 |
| Chain | Residue |
| A | GLN627 |
| A | ASP631 |
| A | LYS646 |
| A | GLN650 |
| A | HOH2887 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B1713 |
| Chain | Residue |
| B | TYR101 |
| B | ARG133 |
| B | SER199 |
| B | LEU200 |
| B | TRP471 |
| B | HOH2311 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B1714 |
| Chain | Residue |
| B | ARG51 |
| B | PRO188 |
| B | ASP192 |
| B | ARG195 |
| B | HOH2302 |
| B | HOH2869 |
| B | HOH2870 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B1715 |
| Chain | Residue |
| B | ASN559 |
| B | HIS594 |
| B | HIS595 |
| B | HOH2871 |
| site_id | CC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B1716 |
| Chain | Residue |
| B | TYR8 |
| B | ASP9 |
| B | LEU12 |
| B | ASP192 |
| B | ARG195 |
| B | ILE196 |
| B | HOH2024 |
| B | HOH2872 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B1717 |
| Chain | Residue |
| A | GLY349 |
| A | LYS350 |
| A | PHE351 |
| B | GLY420 |
| B | GLU421 |
| B | HOH2873 |
| site_id | CC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B1718 |
| Chain | Residue |
| B | HIS130 |
| B | ARG133 |
| B | SER148 |
| B | ARG468 |
| B | TRP471 |
| B | ILE475 |
| B | HOH2597 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:11937059 |
| Chain | Residue | Details |
| A | GLU292 | |
| B | GLU292 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:11937059 |
| Chain | Residue | Details |
| A | ASP365 | |
| A | GLU393 | |
| B | ASP365 | |
| B | GLU393 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLU168 | |
| B | ASN211 | |
| B | LYS288 | |
| B | ARG325 | |
| B | ARG336 | |
| B | LYS360 | |
| B | HIS521 | |
| B | TRP543 | |
| A | ASN211 | |
| A | LYS288 | |
| A | ARG325 | |
| A | ARG336 | |
| A | LYS360 | |
| A | HIS521 | |
| A | TRP543 | |
| B | GLU168 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU387 | |
| B | GLU387 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Participates in a stacking interactions with the sugar rings of 4-O-MeGlcA |
| Chain | Residue | Details |
| A | TRP160 | |
| A | TRP543 | |
| B | TRP160 | |
| B | TRP543 |
