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 | |
| B | TYR247 | |
| B | TRP295 | |
| A | PHE75 | |
| A | TYR247 | |
| A | TRP295 | |
| B | HIS30 | |
| B | PHE75 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| B | GLU175 | |
| B | LEU352 | |
| A | GLU175 | |
| A | LEU352 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Important for substrate recognition => ECO:0000305 |
| Chain | Residue | Details |
| B | TYR299 | |
| B | LEU352 | |
| A | TYR299 | |
| A | LEU352 |
Catalytic Information from CSA
| 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 |
