3CBW
Crystal structure of the YdhT protein from Bacillus subtilis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0006080 | biological_process | substituted mannan metabolic process |
A | 0016985 | molecular_function | mannan endo-1,4-beta-mannosidase activity |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0006080 | biological_process | substituted mannan metabolic process |
B | 0016985 | molecular_function | mannan endo-1,4-beta-mannosidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CIT B 1 |
Chain | Residue |
A | MET117 |
A | SER118 |
A | LYS121 |
A | ASN122 |
B | SER215 |
B | LYS218 |
B | GLN219 |
B | LYS222 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CIT B 2 |
Chain | Residue |
B | HIS370 |
B | HIS368 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CIT B 3 |
Chain | Residue |
B | HIS369 |
B | HIS370 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P49424 |
Chain | Residue | Details |
A | GLU193 | |
B | GLU193 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P49424 |
Chain | Residue | Details |
A | GLU292 | |
B | GLU292 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P49424 |
Chain | Residue | Details |
A | HIS131 | |
A | TRP198 | |
A | TYR268 | |
A | TRP324 | |
B | HIS131 | |
B | TRP198 | |
B | TYR268 | |
B | TRP324 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Plays an important role in maintaining the position of the catalytic nucleophile => ECO:0000250|UniProtKB:P49424 |
Chain | Residue | Details |
A | HIS192 | |
B | HIS192 |