4OAP
An Axe2 mutant (W190I), an acetyl-xylooligosaccharide esterase from Geobacillus Stearmophilus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0004622 | molecular_function | phosphatidylcholine lysophospholipase 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 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 | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 301 |
| Chain | Residue |
| A | SER15 |
| A | GLY63 |
| A | ASN92 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 302 |
| Chain | Residue |
| A | TYR109 |
| A | ASP111 |
| A | HOH419 |
| A | HOH476 |
| A | HOH476 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 303 |
| Chain | Residue |
| B | GLU140 |
| B | GLY141 |
| B | PRO185 |
| B | GOL306 |
| B | HOH410 |
| B | HOH454 |
| A | PRO146 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 304 |
| Chain | Residue |
| A | GLU27 |
| A | GLY28 |
| A | SER29 |
| A | PHE30 |
| A | GLY31 |
| A | ALA32 |
| A | LEU100 |
| A | LYS106 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 305 |
| Chain | Residue |
| A | GLU143 |
| A | ARG148 |
| A | ASP152 |
| A | ASP171 |
| A | GLN173 |
| A | ASN177 |
| A | HOH520 |
| A | HOH558 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 306 |
| Chain | Residue |
| A | LEU180 |
| A | LYS181 |
| A | HOH528 |
| B | GOL302 |
| B | HOH519 |
| B | HOH594 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 307 |
| Chain | Residue |
| A | THR35 |
| A | TYR40 |
| A | PRO195 |
| A | VAL197 |
| A | HIS200 |
| A | HOH497 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 301 |
| Chain | Residue |
| B | SER15 |
| B | GLY63 |
| B | ASN92 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 302 |
| Chain | Residue |
| A | GLU140 |
| A | GLY141 |
| A | PRO185 |
| A | GOL306 |
| A | HOH422 |
| B | HOH594 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 303 |
| Chain | Residue |
| B | PHE169 |
| B | VAL170 |
| B | ASP171 |
| B | GLU210 |
| B | HOH426 |
| B | HOH440 |
| B | HOH497 |
| B | HOH512 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 304 |
| Chain | Residue |
| B | GLU27 |
| B | GLY28 |
| B | SER29 |
| B | LEU33 |
| B | VAL42 |
| B | ILE54 |
| B | ARG55 |
| B | VAL56 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 305 |
| Chain | Residue |
| A | SER196 |
| B | SER29 |
| B | PHE30 |
| B | GLY31 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 306 |
| Chain | Residue |
| A | GOL303 |
| A | HOH534 |
| B | LEU180 |
| B | LYS181 |
| B | HOH454 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 307 |
| Chain | Residue |
| B | CYS19 |
| B | THR35 |
| B | TYR40 |
| B | PRO195 |
| B | HIS200 |
| B | HOH523 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 308 |
| Chain | Residue |
| B | ARG67 |
| B | GLU74 |
| B | GLU105 |
| B | GLU123 |
| B | HOH592 |
| B | HOH600 |
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 |
