4JHL
Crystal Structure of 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 | 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 | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 301 |
| Chain | Residue |
| A | CYS19 |
| A | THR35 |
| A | PRO195 |
| A | SER196 |
| A | VAL197 |
| A | HOH487 |
| A | HOH489 |
| A | HOH528 |
| A | HOH582 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 302 |
| Chain | Residue |
| A | ARG148 |
| A | ASP152 |
| A | ASP171 |
| A | ASN177 |
| A | HOH475 |
| A | HOH580 |
| A | HOH612 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 303 |
| Chain | Residue |
| A | PRO146 |
| A | HOH428 |
| A | HOH442 |
| A | HOH655 |
| B | GLU140 |
| B | GLY141 |
| B | ASN142 |
| B | PRO185 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 304 |
| Chain | Residue |
| A | TYR109 |
| A | ASP111 |
| A | HOH417 |
| A | HOH504 |
| A | HOH504 |
| A | HOH606 |
| A | HOH629 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 305 |
| Chain | Residue |
| A | GLU140 |
| A | GLY141 |
| A | ASN142 |
| A | PRO185 |
| A | HOH433 |
| A | HOH451 |
| B | PRO146 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 306 |
| Chain | Residue |
| A | SER15 |
| A | GLY63 |
| A | ASN92 |
| A | HOH675 |
| A | HOH677 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 307 |
| Chain | Residue |
| A | PHE30 |
| A | GLY31 |
| A | ALA32 |
| A | HOH676 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 301 |
| Chain | Residue |
| B | CYS19 |
| B | THR35 |
| B | PRO195 |
| B | SER196 |
| B | VAL197 |
| B | HIS200 |
| B | HOH476 |
| B | HOH518 |
| B | HOH640 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 302 |
| Chain | Residue |
| B | GLU27 |
| B | GLY28 |
| B | LEU33 |
| B | ARG55 |
| B | VAL56 |
| B | MSE103 |
| B | HOH425 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 303 |
| Chain | Residue |
| B | SER15 |
| B | GLY63 |
| B | ASN92 |
| B | HOH669 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 304 |
| Chain | Residue |
| B | PHE30 |
| B | GLY31 |
| B | ALA32 |
| B | HOH620 |
| B | HOH646 |
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 |
