3VZK
Crystal structure of the Bacillus circulans endo-beta-(1,4)-xylanase (BcX) N35E mutant
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 | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
A | 0045493 | biological_process | xylan catabolic process |
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 | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
B | 0045493 | biological_process | xylan catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 201 |
Chain | Residue |
A | ARG122 |
B | ARG112 |
B | TYR113 |
B | HOH413 |
B | HOH485 |
B | HOH527 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 202 |
Chain | Residue |
B | HOH328 |
B | HOH402 |
B | ASN61 |
B | SER177 |
B | HOH309 |
Functional Information from PROSITE/UniProt
site_id | PS00776 |
Number of Residues | 11 |
Details | GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYVVDsW |
Chain | Residue | Details |
A | PRO75-TRP85 |
site_id | PS00777 |
Number of Residues | 12 |
Details | GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS |
Chain | Residue | Details |
A | MET169-SER180 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:8019418 |
Chain | Residue | Details |
A | GLU78 | |
B | GLU78 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063, ECO:0000269|PubMed:8019418 |
Chain | Residue | Details |
A | GLU172 | |
B | GLU172 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 432 |
Chain | Residue | Details |
A | GLU35 | modifies pKa |
A | TYR69 | electrostatic destabiliser |
A | GLU78 | covalent catalysis, proton shuttle (general acid/base) |
A | TYR80 | modifies pKa |
A | GLU172 | proton shuttle (general acid/base) |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 432 |
Chain | Residue | Details |
B | GLU35 | modifies pKa |
B | TYR69 | electrostatic destabiliser |
B | GLU78 | covalent catalysis, proton shuttle (general acid/base) |
B | TYR80 | modifies pKa |
B | GLU172 | proton shuttle (general acid/base) |