Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003796 | molecular_function | lysozyme activity |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0008152 | biological_process | metabolic process |
| A | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0050829 | biological_process | defense response to Gram-negative bacterium |
| A | 0050830 | biological_process | defense response to Gram-positive bacterium |
| A | 0051672 | biological_process | obsolete catabolism by organism of cell wall peptidoglycan in other organism |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DMS A 201 |
| Chain | Residue |
| A | ASP52 |
| A | GLN57 |
| A | ILE58 |
| A | ASN59 |
| A | TRP63 |
| A | ILE98 |
| A | ALA107 |
| A | DMS204 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DMS A 202 |
| Chain | Residue |
| A | PHE34 |
| A | TRP111 |
| A | ARG114 |
| A | GLY117 |
| A | HOH312 |
| A | ASN27 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE DMS A 203 |
| Chain | Residue |
| A | ASN19 |
| A | GLU35 |
| A | SER36 |
| A | ALA42 |
| A | ASN44 |
| A | ARG68 |
| A | FMT216 |
| A | HOH314 |
| A | HOH346 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DMS A 204 |
| Chain | Residue |
| A | GLU35 |
| A | ASP52 |
| A | GLN57 |
| A | ALA107 |
| A | TRP108 |
| A | VAL109 |
| A | DMS201 |
| A | HOH331 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE DMS A 205 |
| Chain | Residue |
| A | ASN19 |
| A | ARG21 |
| A | GLY22 |
| A | ASN44 |
| A | HOH315 |
| A | HOH341 |
| A | HOH346 |
| A | HOH348 |
| A | HOH351 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE DMS A 206 |
| Chain | Residue |
| A | THR40 |
| A | ALA82 |
| A | LEU83 |
| A | SER85 |
| A | ASP87 |
| A | ILE88 |
| A | ALA90 |
| A | SER91 |
| A | HOH323 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS A 207 |
| Chain | Residue |
| A | SER24 |
| A | LEU25 |
| A | GLY26 |
| A | VAL120 |
| A | ILE124 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DMS A 208 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 209 |
| Chain | Residue |
| A | ASN106 |
| A | ARG112 |
| A | FMT214 |
| A | HOH357 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 210 |
| Chain | Residue |
| A | LYS13 |
| A | ARG14 |
| A | GLY16 |
| A | THR47 |
| A | ARG128 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT A 211 |
| Chain | Residue |
| A | ASN46 |
| A | THR47 |
| A | HOH335 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT A 212 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT A 214 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT A 215 |
| Chain | Residue |
| A | ASP101 |
| A | GLN121 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT A 216 |
| Chain | Residue |
| A | ASN37 |
| A | DMS203 |
| A | HOH356 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT A 217 |
| Chain | Residue |
| A | ARG112 |
| A | LYS116 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 218 |
| Chain | Residue |
| A | GLY4 |
| A | ARG5 |
| A | CYS6 |
| A | GLU7 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FMT A 219 |
| Chain | Residue |
| A | CYS64 |
| A | ASN65 |
| A | ASP66 |
| A | GLY67 |
| A | ARG68 |
| A | THR69 |
| A | SER72 |
| A | NA222 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 220 |
| Chain | Residue |
| A | TYR23 |
| A | GLY104 |
| A | VAL109 |
| A | ASN113 |
| A | HOH351 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT A 221 |
| Chain | Residue |
| A | GLU7 |
| A | ALA11 |
| A | ARG14 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 222 |
| Chain | Residue |
| A | SER72 |
| A | ARG73 |
| A | FMT219 |
| A | HOH353 |
| A | SER60 |
| A | CYS64 |
| site_id | CC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE QPT A 223 |
Functional Information from PROSITE/UniProt
| site_id | PS00128 |
| Number of Residues | 19 |
| Details | GLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnipCsaLlssDItasvnC |
| Chain | Residue | Details |
| A | CYS76-CYS94 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | GLU35 | |
| A | ASP52 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP101 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 203 |
| Chain | Residue | Details |
| A | GLU35 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASN46 | |
| A | ASP48 | |
| A | SER50 | |
| A | ASP52 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction |
| A | ASN59 | |
