1N82
The high-resolution crystal structure of IXT6, a thermophilic, intracellular xylanase from G. stearothermophilus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
| A | 0045493 | biological_process | xylan catabolic process |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
| B | 0045493 | biological_process | xylan catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 401 |
| Chain | Residue |
| A | ASP15 |
| A | ARG282 |
| A | ILE285 |
| A | GLN286 |
| A | HOH4002 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 402 |
| Chain | Residue |
| B | HOH4208 |
| B | ASP1015 |
| B | ARG1282 |
| B | ILE1285 |
| B | GLN1286 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 453 |
| Chain | Residue |
| A | ARG187 |
| A | ASP221 |
| A | ALA225 |
| A | HOH4135 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 455 |
| Chain | Residue |
| A | ASP65 |
| A | LYS125 |
| A | GOL472 |
| A | HOH4113 |
| B | GOL464 |
| B | CYS1113 |
| B | HOH4449 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 461 |
| Chain | Residue |
| A | ALA13 |
| A | ASN14 |
| A | PHE16 |
| A | ARG17 |
| A | GLN286 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 463 |
| Chain | Residue |
| A | GLY124 |
| A | LYS125 |
| A | ILE126 |
| A | ASP169 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 464 |
| Chain | Residue |
| A | ARG120 |
| A | ARG121 |
| A | HOH4055 |
| B | GOL455 |
| B | CYS1113 |
| B | SER1116 |
| B | ARG1120 |
| B | HOH4048 |
| B | HOH4163 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 465 |
| Chain | Residue |
| A | TYR166 |
| A | PRO170 |
| A | HOH4263 |
| A | HOH4461 |
| A | HOH4515 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 466 |
| Chain | Residue |
| B | ASP1138 |
| B | ARG1145 |
| B | TYR1179 |
| B | ASN1180 |
| B | LYS1186 |
| B | HIS1250 |
| B | ASP1251 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 467 |
| Chain | Residue |
| A | ASN2 |
| A | LEU5 |
| A | PRO6 |
| A | ASP36 |
| A | HIS37 |
| A | HOH4079 |
| A | HOH4409 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 469 |
| Chain | Residue |
| A | ASP155 |
| A | GLU159 |
| A | SER196 |
| A | LEU197 |
| A | HOH4088 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 470 |
| Chain | Residue |
| A | GLU134 |
| A | TYR179 |
| A | GLN210 |
| A | HIS212 |
| A | GLU241 |
| A | HOH4017 |
| A | HOH4218 |
| A | HOH4446 |
| A | HOH4487 |
| A | HOH4516 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 472 |
| Chain | Residue |
| A | ASP65 |
| A | ASP69 |
| A | HOH4038 |
| A | HOH4131 |
| A | HOH4517 |
| B | GOL455 |
| B | GOL473 |
| B | GLU1056 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 473 |
| Chain | Residue |
| A | GOL472 |
| A | HOH4517 |
| B | GLU1056 |
| B | ARG1110 |
| B | HOH4065 |
| B | HOH4197 |
| B | HOH4240 |
| B | HOH4443 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 474 |
| Chain | Residue |
| B | TRP1085 |
| B | GLU1134 |
| B | GLN1210 |
| B | HIS1212 |
| B | GLU1241 |
| B | ARG1252 |
| B | TRP1291 |
| B | HOH4090 |
| B | HOH4529 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 476 |
| Chain | Residue |
| B | VAL1068 |
| B | ASP1069 |
| B | TYR1122 |
| B | LYS1125 |
| B | ASP1065 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1exp |
| Chain | Residue | Details |
| A | HIS212 | |
| A | ASP243 | |
| A | GLU134 | |
| A | GLU241 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1exp |
| Chain | Residue | Details |
| B | HIS1212 | |
| B | GLU1241 | |
| B | GLU1134 | |
| B | ASP1243 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1exp |
| Chain | Residue | Details |
| A | GLU134 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1exp |
| Chain | Residue | Details |
| B | GLU1134 |
