1IC7

CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT(HD32A99A)-HEN LYSOZYME COMPLEX

Functional Information from GO Data

Chain	GOid	namespace	contents
H	0002250	biological_process	adaptive immune response
H	0002376	biological_process	immune system process
H	0003823	molecular_function	antigen binding
H	0016064	biological_process	immunoglobulin mediated immune response
H	0019814	cellular_component	immunoglobulin complex
H	0072562	cellular_component	blood microparticle
L	0002250	biological_process	adaptive immune response
L	0002376	biological_process	immune system process
L	0005615	cellular_component	extracellular space
L	0006955	biological_process	immune response
L	0019814	cellular_component	immunoglobulin complex
Y	0003796	molecular_function	lysozyme activity
Y	0003824	molecular_function	catalytic activity
Y	0005515	molecular_function	protein binding
Y	0005576	cellular_component	extracellular region
Y	0005615	cellular_component	extracellular space
Y	0005737	cellular_component	cytoplasm
Y	0005783	cellular_component	endoplasmic reticulum
Y	0008152	biological_process	metabolic process
Y	0016231	molecular_function	beta-N-acetylglucosaminidase activity
Y	0016787	molecular_function	hydrolase activity
Y	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
Y	0016998	biological_process	cell wall macromolecule catabolic process
Y	0031640	biological_process	killing of cells of another organism
Y	0042742	biological_process	defense response to bacterium
Y	0042802	molecular_function	identical protein binding
Y	0050829	biological_process	defense response to Gram-negative bacterium
Y	0050830	biological_process	defense response to Gram-positive bacterium
Y	0051672	biological_process	obsolete catabolism by organism of cell wall peptidoglycan in other organism

Functional Information from PROSITE/UniProt

site_id	PS00128
Number of Residues	19
Details	GLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnipCsaLlssDItasvnC

Chain	Residue	Details
Y	CYS76-CYS94

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE:

Chain	Residue	Details
Y	GLU35
Y	ASP52

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
Y	ASP101

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 203

Chain	Residue	Details
Y	GLU35	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
Y	ASN46
Y	ASP48
Y	SER50
Y	ASP52	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, polar/non-polar interaction
Y	ASN59

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