Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003796 | molecular_function | lysozyme 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 | 0016231 | molecular_function | beta-N-acetylglucosaminidase 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 | 5 |
Details | binding site for residue NO3 A 201 |
Chain | Residue |
A | ASN65 |
A | ASN74 |
A | ASN77 |
A | ILE78 |
A | PRO79 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue NO3 A 202 |
Chain | Residue |
A | ARG68 |
A | THR69 |
A | SER72 |
A | HOH301 |
A | HOH337 |
A | CYS64 |
A | ASN65 |
A | ASP66 |
A | GLY67 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue NO3 A 203 |
Chain | Residue |
A | ARG21 |
A | VAL99 |
A | SER100 |
A | GLY102 |
A | ASN103 |
A | GLY104 |
A | VAL109 |
A | ASN113 |
A | HOH349 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue PT A 204 |
Chain | Residue |
A | LYS1 |
A | GLU7 |
A | DMS212 |
A | HOH316 |
A | HOH373 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue PT A 205 |
Chain | Residue |
A | ARG14 |
A | HIS15 |
A | DMS217 |
A | HOH382 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue PT A 206 |
Chain | Residue |
A | HIS15 |
A | DMS216 |
A | DMS218 |
A | HOH310 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue PT A 207 |
Chain | Residue |
A | LYS13 |
A | LEU129 |
A | LEU129 |
A | DMS214 |
A | DMS214 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue PT A 208 |
Chain | Residue |
A | LYS96 |
A | DMS218 |
A | HOH381 |
A | HOH386 |
A | HOH408 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue PT A 209 |
Chain | Residue |
A | ASN93 |
A | LYS97 |
A | HOH380 |
A | HOH390 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue PT A 210 |
Chain | Residue |
A | ASP101 |
A | HOH304 |
A | HOH402 |
A | HOH411 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue PT A 211 |
Chain | Residue |
A | LYS1 |
A | HOH322 |
A | HOH391 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue DMS A 212 |
Chain | Residue |
A | LYS1 |
A | PT204 |
A | HOH373 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue DMS A 213 |
Chain | Residue |
A | ALA10 |
A | ALA11 |
A | ARG14 |
A | ARG14 |
A | DMS217 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue DMS A 214 |
Chain | Residue |
A | LYS13 |
A | ASP18 |
A | PRO70 |
A | LEU129 |
A | PT207 |
A | PT207 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue DMS A 215 |
Chain | Residue |
A | SER24 |
A | LEU25 |
A | GLY26 |
A | GLN121 |
A | ILE124 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue DMS A 216 |
Chain | Residue |
A | ARG14 |
A | HIS15 |
A | ARG128 |
A | PT206 |
A | DMS218 |
A | HOH331 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue DMS A 217 |
Chain | Residue |
A | LYS1 |
A | GLU7 |
A | ARG14 |
A | PT205 |
A | DMS213 |
A | HOH338 |
site_id | AD9 |
Number of Residues | 7 |
Details | binding site for residue DMS A 218 |
Chain | Residue |
A | ASN93 |
A | LYS96 |
A | ARG128 |
A | PT206 |
A | PT208 |
A | DMS216 |
A | HOH310 |
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 | |