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 | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 206 |
Chain | Residue |
A | SER24 |
A | GLY26 |
A | GLN121 |
A | HOH846 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PDC A 302 |
Chain | Residue |
A | HOH824 |
A | CYS6 |
A | ARG112 |
A | CYS127 |
A | ARG128 |
A | HOH719 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PDC A 303 |
Chain | Residue |
A | GLY4 |
A | ARG5 |
A | CYS6 |
A | GLU7 |
A | TYR20 |
A | LYS96 |
A | LYS97 |
A | HOH720 |
A | HOH726 |
A | HOH728 |
A | HOH768 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PDC A 304 |
Chain | Residue |
A | ASN93 |
A | LYS97 |
A | ARG112 |
A | LYS116 |
A | ARG128 |
A | HOH726 |
A | HOH787 |
A | HOH836 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PDC A 402 |
Chain | Residue |
A | ARG125 |
A | GLY126 |
A | HOH786 |
A | HOH788 |
site_id | BC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PDC A 403 |
Chain | Residue |
A | TYR20 |
A | ARG21 |
A | ARG125 |
A | GLY126 |
A | HOH707 |
A | HOH724 |
A | HOH729 |
A | HOH742 |
A | HOH806 |
A | HOH863 |
A | HOH877 |
site_id | BC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PDC A 404 |
Chain | Residue |
A | TYR20 |
A | ARG21 |
A | ARG125 |
A | GLY126 |
A | HOH707 |
A | HOH724 |
A | HOH729 |
A | HOH742 |
A | HOH806 |
A | HOH863 |
A | HOH877 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PDC A 502 |
Chain | Residue |
A | ARG61 |
A | TRP62 |
A | ARG68 |
A | ARG73 |
A | LEU84 |
A | SER85 |
A | SER86 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PDC A 503 |
Chain | Residue |
A | ARG68 |
A | SER86 |
A | ASN103 |
A | HOH800 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PDC A 504 |
Chain | Residue |
A | TRP62 |
A | HOH843 |
A | HOH880 |
site_id | BC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PDC A 602 |
Chain | Residue |
A | ARG21 |
A | SER100 |
A | ASP101 |
A | GLY102 |
A | ASN103 |
A | GLY104 |
A | ALA122 |
A | HOH780 |
A | HOH844 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PDC A 603 |
Chain | Residue |
A | ARG14 |
A | ARG21 |
A | GLN121 |
A | ARG125 |
A | HOH778 |
A | HOH827 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PDC A 604 |
Chain | Residue |
A | TYR23 |
A | GLY102 |
A | ASN103 |
A | ASN106 |
A | HOH823 |
A | HOH831 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PDC A 702 |
Chain | Residue |
A | ARG21 |
A | GLY22 |
A | TYR23 |
A | HOH822 |
A | HOH831 |
A | HOH835 |
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 | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 132l |
Chain | Residue | Details |
A | GLU35 | |
A | ASP52 | |
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 | |