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1JKC

HUMAN LYSOZYME MUTANT WITH TRP 109 REPLACED BY PHE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006954biological_processinflammatory response
A0008152biological_processmetabolic process
A0016787molecular_functionhydrolase activity
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 NO3 A 131
ChainResidue
AGLU4
AARG5
ACYS6
AGLU7
AHOH159

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 132
ChainResidue
AHOH134
AHOH145
AASN27
AASN66
AASN75
ASER80

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

217705

PDB entries from 2024-03-27

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