8Y1R
in situ room temperature Laue crystallography
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 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 |