6SHY
Structure of L320A/H321S double mutant of Rex8A from Paenibacillus barcinonensis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005975 | biological_process | carbohydrate metabolic process |
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 | 0003824 | molecular_function | catalytic activity |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
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 | ACT_SITE: Proton donor => ECO:0000305|PubMed:27316951 |
Chain | Residue | Details |
A | GLU70 | |
B | GLU70 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:27316951 |
Chain | Residue | Details |
A | ASP265 | |
B | ASP265 |