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1GFE

CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

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 Residues7
DetailsBINDING SITE FOR RESIDUE NA A 601
ChainResidue
ASER61
ACYS65
AASN66
AALA73
AVAL74
AHOH172
AHOH224

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
DetailsAnnotated By Reference To The Literature 132l
ChainResidueDetails
AGLU35
AASP53

226707

PDB entries from 2024-10-30

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