1PZ3
Crystal structure of a family 51 (GH51) alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T6
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000272 | biological_process | polysaccharide catabolic process |
A | 0005737 | cellular_component | cytoplasm |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0031222 | biological_process | arabinan catabolic process |
A | 0046373 | biological_process | L-arabinose metabolic process |
A | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
B | 0000272 | biological_process | polysaccharide catabolic process |
B | 0005737 | cellular_component | cytoplasm |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0031222 | biological_process | arabinan catabolic process |
B | 0046373 | biological_process | L-arabinose metabolic process |
B | 0046556 | molecular_function | alpha-L-arabinofuranosidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 503 |
Chain | Residue |
A | PHE27 |
A | HOH854 |
A | TRP99 |
A | TYR246 |
A | GLU294 |
A | TRP298 |
A | GLN351 |
A | HOH546 |
A | HOH793 |
A | HOH851 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 503 |
Chain | Residue |
B | PHE27 |
B | ASN74 |
B | TRP99 |
B | TYR246 |
B | GLU294 |
B | TRP298 |
B | GLN351 |
B | HOH505 |
B | HOH959 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor |
Chain | Residue | Details |
A | MET176 | |
B | MET176 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
A | TRP295 | |
B | TRP295 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS30 | |
A | PHE75 | |
A | TYR247 | |
A | TRP295 | |
B | HIS30 | |
B | PHE75 | |
B | TYR247 | |
B | TRP295 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLU175 | |
A | LEU352 | |
B | GLU175 | |
B | LEU352 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Important for substrate recognition => ECO:0000305 |
Chain | Residue | Details |
A | TYR299 | |
A | LEU352 | |
B | TYR299 | |
B | LEU352 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details |
Chain | Residue | Details |
A | GLU175 |
site_id | CSA2 |
Number of Residues | 1 |
Details |
Chain | Residue | Details |
B | GLU175 |
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 667 |
Chain | Residue | Details |
A | MET176 | activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
A | TRP295 | covalently attached, nucleofuge, nucleophile |
site_id | MCSA2 |
Number of Residues | 2 |
Details | M-CSA 667 |
Chain | Residue | Details |
B | MET176 | activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
B | TRP295 | covalently attached, nucleofuge, nucleophile |