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 |