4JKO
Crystal structure of a catalytic mutant of Axe2 (Axe2_S15A), 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 | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 301 |
| Chain | Residue |
| A | CYS19 |
| A | THR35 |
| A | PRO195 |
| A | SER196 |
| A | VAL197 |
| A | HOH488 |
| A | HOH526 |
| A | HOH581 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 302 |
| Chain | Residue |
| A | ASP152 |
| A | ASP171 |
| A | ASN177 |
| A | HOH458 |
| A | HOH476 |
| A | HOH579 |
| A | ARG148 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 303 |
| Chain | Residue |
| A | GLU27 |
| A | GLY28 |
| A | SER29 |
| A | PHE30 |
| A | GLY31 |
| A | ALA32 |
| A | LYS106 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 304 |
| Chain | Residue |
| A | MET1 |
| A | LYS125 |
| A | PRO126 |
| A | VAL128 |
| A | HOH521 |
| A | HOH539 |
| A | HOH573 |
| A | HOH637 |
| A | HOH638 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 305 |
| Chain | Residue |
| A | GLU140 |
| A | GLY141 |
| A | PRO185 |
| A | HOH434 |
| A | HOH452 |
| B | PRO146 |
| B | HOH547 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 306 |
| Chain | Residue |
| A | ASP14 |
| A | ALA15 |
| A | GLY63 |
| A | ASN92 |
| A | TRP95 |
| A | HIS194 |
| A | HOH468 |
| A | HOH568 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 301 |
| Chain | Residue |
| B | CYS19 |
| B | THR35 |
| B | PRO195 |
| B | SER196 |
| B | VAL197 |
| B | HOH476 |
| B | HOH519 |
| B | HOH529 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 302 |
| Chain | Residue |
| B | GLY28 |
| B | SER29 |
| B | PHE30 |
| B | GLY31 |
| B | ALA32 |
| B | HOH552 |
| B | HOH618 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 B 303 |
| Chain | Residue |
| B | ASP14 |
| B | ALA15 |
| B | SER62 |
| B | GLY63 |
| B | ASN92 |
| B | TRP95 |
| B | HIS194 |
| B | HOH473 |
| B | HOH508 |
| B | HOH621 |
| B | HOH658 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 304 |
| Chain | Residue |
| B | ARG149 |
| B | GLN153 |
| B | HOH462 |
| B | HOH530 |
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 | ALA15 | |
| B | ALA15 |
| 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 | ASP191 | |
| A | HIS194 | |
| B | ASP191 | |
| 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 |
