3W7V
Crystal Structure of Axe2, 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 | phosphatidylcholine lysophospholipase A1 activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016787 | molecular_function | hydrolase activity |
| 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 | phosphatidylcholine lysophospholipase A1 activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016787 | molecular_function | hydrolase activity |
| 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 | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 301 |
| Chain | Residue |
| A | CYS19 |
| A | THR35 |
| A | PRO195 |
| A | SER196 |
| A | VAL197 |
| A | HOH524 |
| A | HOH594 |
| A | HOH646 |
| A | HOH657 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 302 |
| Chain | Residue |
| A | ASP111 |
| A | HOH415 |
| A | HOH596 |
| A | HOH596 |
| A | HOH599 |
| A | HOH620 |
| A | HOH620 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 303 |
| Chain | Residue |
| A | SER15 |
| A | GLY63 |
| A | ASN92 |
| A | HOH648 |
| A | HOH655 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 301 |
| Chain | Residue |
| A | GLU140 |
| A | GLY141 |
| A | PRO185 |
| A | HOH434 |
| A | HOH444 |
| B | PRO146 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 302 |
| Chain | Residue |
| B | CYS19 |
| B | THR35 |
| B | GLY36 |
| B | PRO195 |
| B | SER196 |
| B | VAL197 |
| B | HOH512 |
| B | HOH522 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 303 |
| Chain | Residue |
| A | ALA186 |
| A | ALA187 |
| A | LEU188 |
| A | ALA189 |
| A | SER196 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 304 |
| Chain | Residue |
| B | SER15 |
| B | GLY63 |
| B | ASN92 |
| B | HOH585 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"21994937","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24531461","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"21994937","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24531461","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"24531461","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
