7DFM
Crystal structure of glycoside hydrolase family 11 beta-xylanase from Streptomyces olivaceoviridis E-86
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| 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 | 0000272 | biological_process | polysaccharide catabolic process |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| 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 |
| C | 0000272 | biological_process | polysaccharide catabolic process |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
| C | 0045493 | biological_process | xylan catabolic process |
| D | 0000272 | biological_process | polysaccharide catabolic process |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
| D | 0045493 | biological_process | xylan catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 401 |
| Chain | Residue |
| A | GLY112 |
| A | THR113 |
| A | SER142 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 402 |
| Chain | Residue |
| A | ASN93 |
| A | THR145 |
| A | HOH531 |
| D | TYR122 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| B | THR100 |
| B | HOH528 |
| D | ASN123 |
| A | SER142 |
| A | LYS143 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 404 |
| Chain | Residue |
| A | SER181 |
| A | SER182 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 405 |
| Chain | Residue |
| A | TYR103 |
| A | ASN123 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 406 |
| Chain | Residue |
| A | ARG144 |
| A | THR148 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 407 |
| Chain | Residue |
| A | GLY95 |
| A | LYS143 |
| B | HOH513 |
| D | TYR122 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 401 |
| Chain | Residue |
| A | GLY111 |
| B | THR130 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 402 |
| Chain | Residue |
| A | TYR97 |
| A | HOH501 |
| B | ARG121 |
| B | TYR122 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 403 |
| Chain | Residue |
| B | THR113 |
| B | SER142 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 404 |
| Chain | Residue |
| B | ASP110 |
| B | ARG144 |
| B | THR148 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 401 |
| Chain | Residue |
| C | THR113 |
| C | SER142 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 402 |
| Chain | Residue |
| C | THR5 |
| C | THR6 |
| C | GLN8 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue CL C 403 |
| Chain | Residue |
| C | THR108 |
| C | ASP110 |
| C | GLY111 |
| D | ASN83 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 404 |
| Chain | Residue |
| A | ASN43 |
| C | ASN12 |
| C | ASN13 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 405 |
| Chain | Residue |
| C | ASP110 |
| C | ARG144 |
| C | THR148 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 406 |
| Chain | Residue |
| C | THR2 |
| C | ASN12 |
| C | LEU31 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 301 |
| Chain | Residue |
| B | GLN141 |
| B | HOH518 |
| D | LEU85 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue CL D 302 |
| Chain | Residue |
| C | THR102 |
| C | HOH507 |
| D | ALA1 |
| D | GLY10 |
| D | THR11 |
| site_id | AE2 |
| Number of Residues | 2 |
| Details | binding site for residue CL D 303 |
| Chain | Residue |
| D | ARG144 |
| D | THR148 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 304 |
| Chain | Residue |
| D | SER66 |
| D | PHE67 |
| D | THR145 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 305 |
| Chain | Residue |
| D | THR113 |
| D | ARG140 |
| D | SER142 |
Functional Information from PROSITE/UniProt
| site_id | PS00776 |
| Number of Residues | 11 |
| Details | GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLvEYYIVDnW |
| Chain | Residue | Details |
| A | PRO84-TRP94 |
| site_id | PS00777 |
| Number of Residues | 12 |
| Details | GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. LatEGYQSSGsS |
| Chain | Residue | Details |
| A | LEU174-SER185 |
