4OAO
A mutant of Axe2 (R55A), and 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 | 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 CL A 301 |
Chain | Residue |
A | SER15 |
A | GLY63 |
A | ASN92 |
A | HOH578 |
A | HOH579 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 302 |
Chain | Residue |
A | HIS200 |
A | HOH411 |
A | THR35 |
A | TYR40 |
A | PRO195 |
A | VAL197 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 303 |
Chain | Residue |
A | TYR109 |
A | ASP111 |
A | HOH432 |
A | HOH433 |
A | HOH549 |
A | HOH549 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 304 |
Chain | Residue |
A | PRO146 |
A | HOH422 |
B | GLU140 |
B | GLY141 |
B | PRO185 |
B | HOH448 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 305 |
Chain | Residue |
A | GLU143 |
A | ARG148 |
A | ASP152 |
A | ASP171 |
A | GLN173 |
A | ASN177 |
A | HOH426 |
A | HOH490 |
A | HOH563 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 301 |
Chain | Residue |
B | SER15 |
B | GLY63 |
B | ASN92 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 302 |
Chain | Residue |
B | CYS19 |
B | THR35 |
B | PRO195 |
B | SER196 |
B | VAL197 |
B | HOH466 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 303 |
Chain | Residue |
A | GLY141 |
A | PRO185 |
A | HOH431 |
B | PRO146 |
B | HOH447 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 304 |
Chain | Residue |
B | PHE169 |
B | ASP171 |
B | GLU210 |
B | HOH430 |
B | HOH515 |
B | HOH524 |
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 | 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 |