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1BB6

LYSOZYME COMPLEX WITH 4-METHYL-UMBELLIFERYL CHITOTRIOSE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE UMG A 130
ChainResidue
AARG97
AASP101
APRO102
AASN103
AALA107
ATRP108
AHOH149
AHOH151
AHOH219
AHOH237
AHOH259
AHOH261
AHOH273
AASN46
AASP52
AILE58
AASN59
ATYR62
ATRP63
AVAL75

site_idNUL
Number of Residues2
DetailsCATALYTICALLY ACTIVE RESIDUES.
ChainResidue
AGLU35
AASP52

Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CgirCsqLltdDLtvairC
ChainResidueDetails
ACYS76-CYS94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AGLU35
AASP52

220113

PDB entries from 2024-05-22

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