5JOW
Bacteroides ovatus Xyloglucan PUL GH43A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
| A | 0085030 | biological_process | symbiotic process benefiting host |
| A | 2000899 | biological_process | xyloglucan catabolic process |
| B | 0000272 | biological_process | polysaccharide catabolic process |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
| B | 0085030 | biological_process | symbiotic process benefiting host |
| B | 2000899 | biological_process | xyloglucan catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue TRS A 601 |
| Chain | Residue |
| A | ASP34 |
| A | EDO603 |
| A | HOH817 |
| A | HOH824 |
| A | PHE51 |
| A | PHE93 |
| A | ALA94 |
| A | ILE139 |
| A | ASP140 |
| A | GLU189 |
| A | ARG283 |
| A | PHE491 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 602 |
| Chain | Residue |
| A | LEU162 |
| A | GLU164 |
| A | SER174 |
| A | SER175 |
| A | LYS177 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 603 |
| Chain | Residue |
| A | GLU189 |
| A | GLY208 |
| A | THR209 |
| A | GLU210 |
| A | TRS601 |
| A | HOH724 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 604 |
| Chain | Residue |
| A | GLU146 |
| A | ASP147 |
| A | LYS149 |
| A | TYR200 |
| A | HOH854 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 605 |
| Chain | Residue |
| A | VAL290 |
| A | ARG291 |
| A | HOH774 |
| A | HOH795 |
| A | HOH845 |
| A | HOH1041 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 606 |
| Chain | Residue |
| A | ASP295 |
| A | HOH702 |
| A | HOH716 |
| A | HOH921 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 607 |
| Chain | Residue |
| A | ASN301 |
| A | ASN303 |
| A | HOH736 |
| A | HOH777 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 608 |
| Chain | Residue |
| A | VAL132 |
| A | TRP133 |
| A | THR169 |
| A | HOH752 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 609 |
| Chain | Residue |
| A | ARG98 |
| A | LEU143 |
| A | HOH759 |
| A | HOH788 |
| A | HOH886 |
| A | HOH892 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 610 |
| Chain | Residue |
| A | ARG178 |
| A | ILE179 |
| A | ASP224 |
| A | GLY225 |
| A | PRO226 |
| A | HOH704 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 611 |
| Chain | Residue |
| A | GLU210 |
| A | THR485 |
| A | GLY490 |
| A | PHE491 |
| A | HOH707 |
| site_id | AD3 |
| Number of Residues | 12 |
| Details | binding site for residue TRS B 601 |
| Chain | Residue |
| B | ASP34 |
| B | PHE51 |
| B | PHE93 |
| B | ALA94 |
| B | ILE139 |
| B | ASP140 |
| B | GLU189 |
| B | ARG283 |
| B | PHE491 |
| B | EDO609 |
| B | HOH792 |
| B | HOH813 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 602 |
| Chain | Residue |
| B | GLU69 |
| B | GLN70 |
| B | LYS321 |
| B | GLU337 |
| B | HOH703 |
| B | HOH730 |
| B | HOH1140 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 603 |
| Chain | Residue |
| B | ILE71 |
| B | GLY72 |
| B | ASN73 |
| B | PRO124 |
| B | ARG125 |
| B | SER126 |
| B | HOH877 |
| B | HOH1063 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 604 |
| Chain | Residue |
| B | ASN87 |
| B | SER88 |
| B | GLU408 |
| B | HOH729 |
| B | HOH757 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 605 |
| Chain | Residue |
| B | HOH899 |
| B | HOH968 |
| B | ARG98 |
| B | LEU143 |
| B | HOH727 |
| B | HOH739 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 606 |
| Chain | Residue |
| B | GLU146 |
| B | ASP147 |
| B | TYR200 |
| B | HOH920 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 607 |
| Chain | Residue |
| B | LEU162 |
| B | GLU164 |
| B | SER174 |
| B | SER175 |
| B | LYS177 |
| B | HOH793 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 608 |
| Chain | Residue |
| B | ASP166 |
| B | MET168 |
| B | HOH819 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 609 |
| Chain | Residue |
| B | GLU189 |
| B | GLY208 |
| B | THR209 |
| B | GLU210 |
| B | TRS601 |
| site_id | AE3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 610 |
| Chain | Residue |
| B | VAL290 |
| B | ARG291 |
| B | HOH798 |
| B | HOH807 |
| B | HOH816 |
| B | HOH961 |
| B | HOH1143 |
| site_id | AE4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 611 |
| Chain | Residue |
| B | LYS309 |
| B | ASP311 |
| B | HOH770 |
| B | HOH831 |
| site_id | AE5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 612 |
| Chain | Residue |
| B | VAL390 |
| B | VAL391 |
| B | LEU392 |
| B | VAL417 |
| B | ARG425 |
| B | HOH721 |
| B | HOH986 |
| site_id | AE6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 613 |
| Chain | Residue |
| B | SER426 |
| B | GLU442 |
| B | SER444 |
| B | HOH747 |
| site_id | AE7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 614 |
| Chain | Residue |
| B | LYS456 |
| B | TYR472 |
| B | ASP474 |
| B | HOH873 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"27466444","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"27466444","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate","evidences":[{"source":"PubMed","id":"27466444","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
