3LK6
Beta-N-hexosaminidase N318D mutant (YBBD_N318D) from bacillus subtilis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004563 | molecular_function | beta-N-acetylhexosaminidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0009254 | biological_process | peptidoglycan turnover |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0071555 | biological_process | cell wall organization |
| A | 0102148 | molecular_function | N-acetyl-beta-D-galactosaminidase activity |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0004563 | molecular_function | beta-N-acetylhexosaminidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0009254 | biological_process | peptidoglycan turnover |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0071555 | biological_process | cell wall organization |
| B | 0102148 | molecular_function | N-acetyl-beta-D-galactosaminidase activity |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0004563 | molecular_function | beta-N-acetylhexosaminidase activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0008360 | biological_process | regulation of cell shape |
| C | 0009252 | biological_process | peptidoglycan biosynthetic process |
| C | 0009254 | biological_process | peptidoglycan turnover |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0071555 | biological_process | cell wall organization |
| C | 0102148 | molecular_function | N-acetyl-beta-D-galactosaminidase activity |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0004563 | molecular_function | beta-N-acetylhexosaminidase activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0008360 | biological_process | regulation of cell shape |
| D | 0009252 | biological_process | peptidoglycan biosynthetic process |
| D | 0009254 | biological_process | peptidoglycan turnover |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0071555 | biological_process | cell wall organization |
| D | 0102148 | molecular_function | N-acetyl-beta-D-galactosaminidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 643 |
| Chain | Residue |
| A | LYS479 |
| A | ILE481 |
| A | LYS482 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 644 |
| Chain | Residue |
| A | ASN152 |
| A | GLN155 |
| A | LYS429 |
| A | LYS433 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG A 645 |
| Chain | Residue |
| A | HIS222 |
| A | ASN318 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 646 |
| Chain | Residue |
| A | ARG148 |
| A | SER149 |
| A | ARG150 |
| A | ILE151 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 647 |
| Chain | Residue |
| A | THR106 |
| A | ASP107 |
| A | LEU167 |
| A | GLY168 |
| A | LYS410 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG B 643 |
| Chain | Residue |
| B | LYS479 |
| B | ILE481 |
| B | LYS482 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG B 644 |
| Chain | Residue |
| B | ARG148 |
| B | SER149 |
| B | ARG150 |
| B | ILE151 |
| B | ARG202 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PEG B 645 |
| Chain | Residue |
| B | ILE151 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG B 648 |
| Chain | Residue |
| B | HIS222 |
| B | ASN318 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG B 649 |
| Chain | Residue |
| B | ASN182 |
| B | ASP184 |
| B | ASP230 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG B 650 |
| Chain | Residue |
| B | ASN152 |
| B | GLN155 |
| B | LYS429 |
| B | LYS433 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 651 |
| Chain | Residue |
| B | THR106 |
| B | ASP107 |
| B | LEU167 |
| B | GLY168 |
| B | LYS410 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PEG C 647 |
| Chain | Residue |
| C | THR280 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG C 643 |
| Chain | Residue |
| C | LYS479 |
| C | ILE481 |
| C | LYS482 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG C 644 |
| Chain | Residue |
| C | ARG148 |
| C | SER149 |
| C | ARG150 |
| C | ILE151 |
| C | ARG202 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG C 645 |
| Chain | Residue |
| C | ASN152 |
| C | GLN155 |
| C | ALA426 |
| C | LYS429 |
| C | LYS433 |
| site_id | BC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PEG C 646 |
| Chain | Residue |
| C | HIS222 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA C 648 |
| Chain | Residue |
| C | THR106 |
| C | ASP107 |
| C | GLY168 |
| C | LYS410 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG D 643 |
| Chain | Residue |
| D | HIS222 |
| D | HIS226 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG D 644 |
| Chain | Residue |
| D | ASN152 |
| D | GLN155 |
| D | LYS429 |
| D | LYS433 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG D 645 |
| Chain | Residue |
| D | ARG148 |
| D | SER149 |
| D | ARG150 |
| D | ILE151 |
| D | ARG202 |
| site_id | CC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG D 646 |
| Chain | Residue |
| D | LYS479 |
| D | LYS482 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA D 647 |
| Chain | Residue |
| D | THR106 |
| D | ASP107 |
| D | LEU167 |
| D | GLY168 |
| D | LYS410 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:20826810, ECO:0000305|PubMed:23177201 |
| Chain | Residue | Details |
| A | HIS234 | |
| B | HIS234 | |
| C | HIS234 | |
| D | HIS234 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:20826810, ECO:0000305|PubMed:23177201 |
| Chain | Residue | Details |
| A | ASN318 | |
| B | ASN318 | |
| C | ASN318 | |
| D | ASN318 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20826810, ECO:0000269|PubMed:23177201 |
| Chain | Residue | Details |
| A | ASP123 | |
| C | ARG131 | |
| C | ARG191 | |
| C | LYS221 | |
| D | ASP123 | |
| D | ARG131 | |
| D | ARG191 | |
| D | LYS221 | |
| A | ARG131 | |
| A | ARG191 | |
| A | LYS221 | |
| B | ASP123 | |
| B | ARG131 | |
| B | ARG191 | |
| B | LYS221 | |
| C | ASP123 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Important for catalytic activity => ECO:0000305|PubMed:20826810 |
| Chain | Residue | Details |
| A | ASP232 | |
| B | ASP232 | |
| C | ASP232 | |
| D | ASP232 |
