4JJ4
Crystal structure of a catalytic mutant of Axe2 (Axe2-D191A), an acetylxylan esterase from Geobacillus stearothermophilus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0004622 | molecular_function | lysophospholipase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0045493 | biological_process | xylan catabolic process |
| A | 0046555 | molecular_function | acetylxylan esterase activity |
| A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| B | 0000272 | biological_process | polysaccharide catabolic process |
| B | 0004622 | molecular_function | lysophospholipase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0045493 | biological_process | xylan catabolic process |
| B | 0046555 | molecular_function | acetylxylan esterase activity |
| B | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 301 |
| Chain | Residue |
| A | GLU27 |
| A | GLY28 |
| A | SER29 |
| A | VAL56 |
| A | HOH421 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 302 |
| Chain | Residue |
| B | GLY141 |
| B | PRO185 |
| B | HOH412 |
| A | PRO146 |
| A | HOH436 |
| A | HOH452 |
| B | GLU140 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 303 |
| Chain | Residue |
| A | TYR109 |
| A | TYR109 |
| A | ASP111 |
| A | HOH425 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 304 |
| Chain | Residue |
| A | SER15 |
| A | GLY63 |
| A | ASN92 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 301 |
| Chain | Residue |
| B | GLU27 |
| B | GLY28 |
| B | ILE54 |
| B | ARG55 |
| B | VAL56 |
| B | MET103 |
| B | HOH531 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 302 |
| Chain | Residue |
| A | ALA191 |
| A | ARG192 |
| B | ALA191 |
| B | ARG192 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 303 |
| Chain | Residue |
| B | SER15 |
| B | GLY63 |
| B | ASN92 |
| B | HOH542 |
| B | HOH543 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:21994937, ECO:0000305|PubMed:24531461 |
| Chain | Residue | Details |
| A | SER15 | |
| B | SER15 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Charge relay system => ECO:0000305|PubMed:21994937, ECO:0000305|PubMed:24531461 |
| Chain | Residue | Details |
| A | ALA191 | |
| A | HIS194 | |
| B | ALA191 | |
| B | HIS194 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:24531461 |
| Chain | Residue | Details |
| A | GLY63 | |
| A | ASN92 | |
| B | GLY63 | |
| B | ASN92 |
