2DCY
Crystal structure of Bacillus subtilis family-11 xylanase
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 |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| 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 | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| 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 |
| E | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| E | 0005975 | biological_process | carbohydrate metabolic process |
| E | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| E | 0031176 | molecular_function | endo-1,4-beta-xylanase activity |
| E | 0045493 | biological_process | xylan catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DIO C 601 |
| Chain | Residue |
| C | TRP9 |
| C | TYR69 |
| C | PRO116 |
| C | SER117 |
| C | TYR166 |
| C | HOH638 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DIO A 602 |
| Chain | Residue |
| B | TRP30 |
| A | ASN29 |
| A | TRP30 |
| B | ASN29 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DIO B 603 |
| Chain | Residue |
| A | ILE15 |
| A | ASN17 |
| A | ASN29 |
| A | TRP30 |
| A | SER31 |
| B | ILE15 |
| B | ASN17 |
| B | ASN29 |
| B | TRP30 |
| B | SER31 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TAR E 501 |
| Chain | Residue |
| A | SER134 |
| A | LYS135 |
| E | SER74 |
| E | LYS99 |
| E | SER100 |
| E | ASP101 |
| E | GLY102 |
| E | GLY103 |
| E | HOH528 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE TAR B 502 |
| Chain | Residue |
| B | ASN8 |
| B | VAL16 |
| B | ASN17 |
| B | ALA18 |
| B | TYR113 |
| B | TLA505 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE TAR B 503 |
| Chain | Residue |
| A | GLN175 |
| A | SER176 |
| A | HOH610 |
| B | TYR65 |
| B | TYR88 |
| B | PRO90 |
| B | THR91 |
| B | THR110 |
| B | ARG112 |
| B | GLN127 |
| B | TRP129 |
| B | HOH630 |
| B | HOH633 |
| B | HOH639 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE TAR A 504 |
| Chain | Residue |
| A | SER100 |
| A | ASP101 |
| A | GLY102 |
| A | ASN148 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TAR B 505 |
| Chain | Residue |
| B | TRP6 |
| B | ASN8 |
| B | ALA18 |
| B | TYR113 |
| B | TLA502 |
| C | SER134 |
| C | LYS135 |
| C | HOH644 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TAR C 506 |
| Chain | Residue |
| A | ALA1 |
| C | THR3 |
| C | ASP4 |
| C | TYR5 |
| C | ASN20 |
| C | SER22 |
| C | GLY23 |
| C | GLY24 |
| C | LYS40 |
| C | HOH634 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TAR A 507 |
| Chain | Residue |
| A | TRP58 |
| A | SER84 |
| A | TRP85 |
| A | LYS135 |
| A | HOH607 |
| A | HOH619 |
| A | HOH626 |
| E | VAL98 |
| E | ASN148 |
| E | ASN151 |
| E | ALA152 |
Functional Information from PROSITE/UniProt
| site_id | PS00776 |
| Number of Residues | 11 |
| Details | GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYVVDsW |
| Chain | Residue | Details |
| A | PRO75-TRP85 |
| site_id | PS00777 |
| Number of Residues | 12 |
| Details | GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS |
| Chain | Residue | Details |
| A | MET169-SER180 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:7911679 |
| Chain | Residue | Details |
| A | GLU78 | |
| B | GLU78 | |
| C | GLU78 | |
| D | GLU78 | |
| E | GLU78 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063 |
| Chain | Residue | Details |
| A | GLU172 | |
| B | GLU172 | |
| C | GLU172 | |
| D | GLU172 | |
| E | GLU172 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bvv |
| Chain | Residue | Details |
| A | GLU172 | |
| A | GLU78 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bvv |
| Chain | Residue | Details |
| B | GLU172 | |
| B | GLU78 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bvv |
| Chain | Residue | Details |
| C | GLU172 | |
| C | GLU78 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bvv |
| Chain | Residue | Details |
| D | GLU172 | |
| D | GLU78 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bvv |
| Chain | Residue | Details |
| E | GLU172 | |
| E | GLU78 |
