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9FGY

Cryo-EM structure of Lysozyme homo-dimer assembled by homo Di-Gluebody - Local refinement

Functional Information from GO Data
ChainGOidnamespacecontents
D0003796molecular_functionlysozyme activity
D0003824molecular_functioncatalytic activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005737cellular_componentcytoplasm
D0005783cellular_componentendoplasmic reticulum
D0005794cellular_componentGolgi apparatus
D0016231molecular_functionbeta-N-acetylglucosaminidase activity
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0016998biological_processcell wall macromolecule catabolic process
D0031640biological_processkilling of cells of another organism
D0042742biological_processdefense response to bacterium
D0042802molecular_functionidentical protein binding
D0050829biological_processdefense response to Gram-negative bacterium
D0050830biological_processdefense response to Gram-positive bacterium
D0051672biological_processobsolete catabolism by organism of cell wall peptidoglycan in other organism
Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnipCsaLlssDItasvnC
ChainResidueDetails
DCYS76-CYS94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 203
ChainResidueDetails

247536

PDB entries from 2026-01-14

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