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1LZ1

REFINEMENT OF HUMAN LYSOZYME AT 1.5 ANGSTROMS RESOLUTION. ANALYSIS OF NON-BONDED AND HYDROGEN-BOND INTERACTIONS

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006954biological_processinflammatory response
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019730biological_processantimicrobial humoral response
A0031640biological_processkilling of cells of another organism
A0035578cellular_componentazurophil granule lumen
A0035580cellular_componentspecific granule lumen
A0042742biological_processdefense response to bacterium
A0042802molecular_functionidentical protein binding
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
A0070062cellular_componentextracellular exosome
A1904724cellular_componenttertiary granule lumen
Functional Information from PDB Data
site_id51
Number of Residues1
Details
ChainResidue
AGLU35

site_id52
Number of Residues1
Details
ChainResidue
AASP53

Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. ChlsCsaLlqdNIadavaC
ChainResidueDetails
ACYS77-CYS95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AGLU35
AASP53

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 8535779
ChainResidueDetails
AGLU35
AASP53

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PDB entries from 2024-11-06

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