6KKA
Xylanase J mutant from Bacillus sp. 41M-1
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 |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0030246 | molecular_function | carbohydrate binding |
A | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
A | 0045493 | biological_process | xylan catabolic process |
A | 0046872 | molecular_function | metal ion binding |
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 | 0030246 | molecular_function | carbohydrate binding |
B | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
B | 0045493 | biological_process | xylan catabolic process |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue CA A 401 |
Chain | Residue |
A | GLU213 |
A | GLU215 |
A | ASN232 |
A | ASP322 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue CA A 402 |
Chain | Residue |
A | TYR237 |
A | ASP313 |
A | TRP317 |
A | ASP318 |
A | HOH519 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue CA A 403 |
Chain | Residue |
A | ASN44 |
A | GLU183 |
A | HOH505 |
A | HOH620 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue CA A 404 |
Chain | Residue |
A | GLN186 |
A | HOH512 |
A | HOH572 |
A | HOH585 |
A | HOH623 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue EPE A 405 |
Chain | Residue |
A | ARG269 |
A | ASP271 |
A | ASN278 |
A | THR281 |
A | THR311 |
A | ALA312 |
A | HOH544 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue GOL A 406 |
Chain | Residue |
A | LYS19 |
A | GLY23 |
A | HOH562 |
A | HOH571 |
B | ASN41 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue GOL A 407 |
Chain | Residue |
A | GLY12 |
A | LYS51 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue GOL A 408 |
Chain | Residue |
A | SER24 |
A | GLY25 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue GOL A 409 |
Chain | Residue |
A | ASN78 |
A | THR228 |
A | ASN232 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue MPD A 410 |
Chain | Residue |
A | GLU16 |
A | TRP18 |
A | ARG48 |
A | TYR84 |
A | TRP86 |
A | ILE134 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue MPD A 412 |
Chain | Residue |
A | TYR80 |
A | ARG128 |
A | GLN142 |
A | TRP144 |
A | HOH529 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue CA B 401 |
Chain | Residue |
B | GLU213 |
B | GLU215 |
B | ASN232 |
B | ASP322 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue CA B 402 |
Chain | Residue |
B | TYR237 |
B | ASP313 |
B | TRP317 |
B | ASP318 |
B | HOH541 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue CA B 403 |
Chain | Residue |
B | ASN44 |
B | GLU183 |
B | HOH552 |
B | HOH565 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue EPE B 404 |
Chain | Residue |
B | ARG269 |
B | ASP271 |
B | ASN278 |
B | THR311 |
B | GOL409 |
B | HOH548 |
site_id | AD7 |
Number of Residues | 7 |
Details | binding site for residue CIT B 405 |
Chain | Residue |
B | TYR80 |
B | ARG128 |
B | GLN142 |
B | GLU183 |
B | TYR185 |
B | SER229 |
B | HOH565 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue GOL B 406 |
Chain | Residue |
B | GLU16 |
B | ARG48 |
B | TYR84 |
site_id | AD9 |
Number of Residues | 2 |
Details | binding site for residue GOL B 407 |
Chain | Residue |
B | ASN78 |
B | ASN232 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue GOL B 408 |
Chain | Residue |
B | SER24 |
B | GLN38 |
B | TRP39 |
B | SER40 |
site_id | AE2 |
Number of Residues | 4 |
Details | binding site for residue GOL B 409 |
Chain | Residue |
A | GLY302 |
A | ASN303 |
B | THR311 |
B | EPE404 |
site_id | AE3 |
Number of Residues | 3 |
Details | binding site for residue GOL B 410 |
Chain | Residue |
B | ASN266 |
B | HOH521 |
B | HOH584 |
site_id | AE4 |
Number of Residues | 5 |
Details | binding site for residue MPD B 411 |
Chain | Residue |
A | GLY23 |
A | SER40 |
B | GLY23 |
B | SER24 |
B | SER40 |
site_id | AE5 |
Number of Residues | 6 |
Details | binding site for residue MPD B 412 |
Chain | Residue |
B | TYR13 |
B | LEU198 |
A | ASP11 |
A | GLY12 |
A | HOH550 |
B | GLY12 |
Functional Information from PROSITE/UniProt
site_id | PS00776 |
Number of Residues | 11 |
Details | GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLvEFYIVDsW |
Chain | Residue | Details |
A | PRO90-TRP100 |
site_id | PS00777 |
Number of Residues | 12 |
Details | GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. LtvEGYQSSGsA |
Chain | Residue | Details |
A | LEU180-ALA191 |