3RO8
Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| E | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| E | 0005975 | biological_process | carbohydrate metabolic process |
| F | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| F | 0005975 | biological_process | carbohydrate metabolic process |
| G | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| G | 0005975 | biological_process | carbohydrate metabolic process |
| H | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| H | 0005975 | biological_process | carbohydrate metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | ASP14 |
| A | ALA296 |
| A | ILE299 |
| A | HOH611 |
| A | HOH859 |
| A | HOH895 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 402 |
| Chain | Residue |
| A | TYR235 |
| A | HOH508 |
| A | GLU196 |
| A | GLN232 |
| A | GLY233 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 403 |
| Chain | Residue |
| A | ASN182 |
| A | PRO183 |
| A | SER184 |
| A | HOH609 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 401 |
| Chain | Residue |
| B | ASP14 |
| B | ALA296 |
| B | ILE299 |
| B | HOH541 |
| B | HOH640 |
| B | HOH947 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 402 |
| Chain | Residue |
| B | GLU196 |
| B | GLN232 |
| B | GLY233 |
| B | TYR235 |
| B | HOH882 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 403 |
| Chain | Residue |
| B | THR60 |
| B | PHE61 |
| B | THR62 |
| C | ASN243 |
| C | HOH812 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 401 |
| Chain | Residue |
| C | ASP14 |
| C | ALA296 |
| C | ILE299 |
| C | HOH551 |
| G | LEU273 |
| G | PRO274 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL C 402 |
| Chain | Residue |
| C | GLU196 |
| C | GLN232 |
| C | GLY233 |
| C | TYR235 |
| C | HOH941 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 401 |
| Chain | Residue |
| D | ASP14 |
| D | ALA296 |
| D | ILE299 |
| D | HOH775 |
| D | HOH900 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL D 402 |
| Chain | Residue |
| D | GLU196 |
| D | GLN232 |
| D | GLY233 |
| D | TYR235 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 401 |
| Chain | Residue |
| E | ASP14 |
| E | ALA296 |
| E | ILE299 |
| E | HOH625 |
| E | HOH866 |
| E | HOH887 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL E 402 |
| Chain | Residue |
| E | GLU196 |
| E | GLN232 |
| E | GLY233 |
| E | TYR235 |
| E | HOH809 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL E 403 |
| Chain | Residue |
| A | ASN100 |
| E | ASN141 |
| E | GLN156 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 404 |
| Chain | Residue |
| E | ASN141 |
| E | PRO144 |
| E | HOH545 |
| E | HOH907 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 401 |
| Chain | Residue |
| F | ASP14 |
| F | ALA296 |
| F | ILE299 |
| F | HOH640 |
| F | HOH823 |
| F | HOH824 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL F 402 |
| Chain | Residue |
| F | GLU196 |
| F | GLN232 |
| F | GLY233 |
| F | TYR235 |
| F | HOH874 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG G 401 |
| Chain | Residue |
| G | ASP14 |
| G | ALA296 |
| G | ILE299 |
| G | HOH574 |
| G | HOH837 |
| G | HOH892 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL G 402 |
| Chain | Residue |
| G | GLU196 |
| G | GLN232 |
| G | GLY233 |
| G | TYR235 |
| G | HOH506 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG H 401 |
| Chain | Residue |
| H | ASP14 |
| H | ALA296 |
| H | ILE299 |
| H | HOH571 |
| H | HOH615 |
| H | HOH774 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL H 402 |
| Chain | Residue |
| H | GLY233 |
| H | TYR235 |
| H | HOH829 |
| H | GLU196 |
| H | GLN232 |
Functional Information from PROSITE/UniProt
| site_id | PS00591 |
| Number of Residues | 11 |
| Details | GH10_1 Glycosyl hydrolases family 10 (GH10) active site. GVEVsVSELDV |
| Chain | Residue | Details |
| A | GLY255-VAL265 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10061","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
