Functional Information from GO Data
Chain | GOid | namespace | contents |
L | 0003796 | molecular_function | lysozyme activity |
L | 0005515 | molecular_function | protein binding |
L | 0005576 | cellular_component | extracellular region |
L | 0005615 | cellular_component | extracellular space |
L | 0005737 | cellular_component | cytoplasm |
L | 0005783 | cellular_component | endoplasmic reticulum |
L | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
L | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
L | 0016998 | biological_process | cell wall macromolecule catabolic process |
L | 0031640 | biological_process | killing of cells of another organism |
L | 0042742 | biological_process | defense response to bacterium |
L | 0042802 | molecular_function | identical protein binding |
L | 0050829 | biological_process | defense response to Gram-negative bacterium |
L | 0050830 | biological_process | defense response to Gram-positive bacterium |
L | 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 | 6 |
Details | BINDING SITE FOR RESIDUE NA A 301 |
Chain | Residue |
A | ASP99 |
A | THR101 |
A | GLY119 |
A | ASP121 |
A | HOH467 |
A | HOH507 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA L 302 |
Chain | Residue |
L | ARG73 |
L | HOH454 |
L | HOH455 |
L | SER60 |
L | CYS64 |
L | SER72 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA L 304 |
Chain | Residue |
L | TYR20 |
L | LYS96 |
L | VAL99 |
L | SER100 |
L | FMT406 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA L 305 |
Chain | Residue |
L | GLU35 |
L | FMT404 |
L | HOH440 |
L | HOH441 |
L | HOH472 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA A 306 |
Chain | Residue |
A | ASN74 |
A | ASN77 |
A | HOH415 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 307 |
Chain | Residue |
A | GLY42 |
L | ARG21 |
L | SER100 |
L | ASP101 |
L | ASN103 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT L 401 |
Chain | Residue |
L | ALA42 |
L | ASN44 |
L | ARG68 |
L | HOH442 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FMT L 402 |
Chain | Residue |
L | ASN65 |
L | GLY67 |
L | ARG68 |
L | THR69 |
L | PRO70 |
L | SER72 |
L | HOH454 |
L | HOH455 |
L | HOH478 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FMT A 403 |
Chain | Residue |
A | ALA6 |
A | TYR94 |
A | TYR95 |
A | CYS96 |
A | GLY124 |
A | GLY126 |
A | THR127 |
A | HOH419 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT L 404 |
Chain | Residue |
A | SER105 |
A | HOH471 |
L | GLU35 |
L | VAL109 |
L | ALA110 |
L | NA305 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT L 405 |
Chain | Residue |
A | GLN39 |
A | HOH492 |
L | TYR20 |
L | ARG21 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT L 406 |
Chain | Residue |
L | TYR20 |
L | LYS96 |
L | LYS97 |
L | NA304 |
L | HOH488 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT L 407 |
Chain | Residue |
A | TYR106 |
L | ARG45 |
L | ASN46 |
L | THR47 |
L | HOH470 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT L 408 |
Chain | Residue |
L | GLY4 |
L | ARG5 |
L | CYS6 |
L | GLU7 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT L 409 |
Chain | Residue |
A | ILE29 |
A | HOH505 |
L | ARG5 |
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 |
L | CYS76-CYS94 | |
site_id | PS00879 |
Number of Residues | 17 |
Details | ODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. Gkereg.VaAINMGGGIT |
Chain | Residue | Details |
A | GLY42-THR58 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: |
Chain | Residue | Details |
L | GLU35 | |
L | ASP52 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: |
Chain | Residue | Details |
L | ASP101 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 132l |
Chain | Residue | Details |
L | GLU35 | |
L | ASP52 | |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 203 |
Chain | Residue | Details |
L | GLU35 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
L | ASN46 | |
L | ASP48 | |
L | SER50 | |
L | ASP52 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction |
L | ASN59 | |