6SHY
Structure of L320A/H321S double mutant of Rex8A from Paenibacillus barcinonensis
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 | 0033951 | molecular_function | oligosaccharide reducing-end xylanase activity |
| A | 0045493 | biological_process | xylan 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 | 0033951 | molecular_function | oligosaccharide reducing-end xylanase activity |
| B | 0045493 | biological_process | xylan catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 401 |
| Chain | Residue |
| A | PHE132 |
| A | HIS201 |
| A | ASN272 |
| A | TYR377 |
| A | EDO402 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | PHE132 |
| A | ALA271 |
| A | EDO401 |
| A | HOH550 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | HIS101 |
| A | THR102 |
| A | GLU103 |
| A | ARG120 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | SER298 |
| A | ASP340 |
| B | GLU313 |
| B | HOH611 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | LYS85 |
| A | HIS86 |
| A | HOH556 |
| A | HOH558 |
| B | ASP89 |
| B | TYR151 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | ARG68 |
| A | TRP112 |
| A | ALA126 |
| A | ASP128 |
| A | TYR197 |
| A | HOH501 |
| A | HOH543 |
| A | HOH662 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | PRO235 |
| A | HOH656 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | ARG68 |
| A | TYR243 |
| A | HOH544 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 409 |
| Chain | Residue |
| A | SER264 |
| A | SER321 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 410 |
| Chain | Residue |
| A | GLU242 |
| A | ASP258 |
| A | PHE259 |
| A | TYR263 |
| A | ARG307 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 401 |
| Chain | Residue |
| B | PHE132 |
| B | HIS201 |
| B | ASN272 |
| B | TYR377 |
| B | EDO402 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | PHE132 |
| B | PHE368 |
| B | EDO401 |
| B | HOH533 |
| B | HOH558 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | HIS101 |
| B | THR102 |
| B | GLU103 |
| B | ARG120 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| A | GLY312 |
| A | GLU313 |
| B | ALA295 |
| B | SER298 |
| B | ASP340 |
| B | HOH556 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 405 |
| Chain | Residue |
| A | ASP89 |
| A | TYR151 |
| B | LYS85 |
| B | HIS86 |
| B | HOH537 |
| B | HOH586 |
| site_id | AD7 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 406 |
| Chain | Residue |
| B | EDO407 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 407 |
| Chain | Residue |
| A | GLN288 |
| B | PRO235 |
| B | EDO406 |
| B | HOH505 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 408 |
| Chain | Residue |
| B | THR231 |
| B | PRO250 |
| B | HOH534 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"27316951","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":"27316951","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
