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1IWT

Crystal Structure Analysis of Human lysozyme at 113K.

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_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 131
ChainResidue
AASP87
AASN88
AHOH236
AHOH350
AHOH355

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 132
ChainResidue
ASER80
AARG107

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 133
ChainResidue
AASN27
AASN66

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

220113

PDB entries from 2024-05-22

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