4AU4

Crystal Structure of Hsp47

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004867	molecular_function	serine-type endopeptidase inhibitor activity
A	0005518	molecular_function	collagen binding
A	0005581	cellular_component	collagen trimer
A	0005615	cellular_component	extracellular space
A	0005783	cellular_component	endoplasmic reticulum
B	0004867	molecular_function	serine-type endopeptidase inhibitor activity
B	0005518	molecular_function	collagen binding
B	0005581	cellular_component	collagen trimer
B	0005615	cellular_component	extracellular space
B	0005783	cellular_component	endoplasmic reticulum
C	0004867	molecular_function	serine-type endopeptidase inhibitor activity
C	0005518	molecular_function	collagen binding
C	0005581	cellular_component	collagen trimer
C	0005615	cellular_component	extracellular space
C	0005783	cellular_component	endoplasmic reticulum
D	0004867	molecular_function	serine-type endopeptidase inhibitor activity
D	0005518	molecular_function	collagen binding
D	0005581	cellular_component	collagen trimer
D	0005615	cellular_component	extracellular space
D	0005783	cellular_component	endoplasmic reticulum
E	0004867	molecular_function	serine-type endopeptidase inhibitor activity
E	0005518	molecular_function	collagen binding
E	0005581	cellular_component	collagen trimer
E	0005615	cellular_component	extracellular space
E	0005783	cellular_component	endoplasmic reticulum
F	0004867	molecular_function	serine-type endopeptidase inhibitor activity
F	0005518	molecular_function	collagen binding
F	0005581	cellular_component	collagen trimer
F	0005615	cellular_component	extracellular space
F	0005783	cellular_component	endoplasmic reticulum
G	0004867	molecular_function	serine-type endopeptidase inhibitor activity
G	0005518	molecular_function	collagen binding
G	0005581	cellular_component	collagen trimer
G	0005615	cellular_component	extracellular space
G	0005783	cellular_component	endoplasmic reticulum

Functional Information from PROSITE/UniProt

site_id	PS00284
Number of Residues	11
Details	SERPIN Serpins signature. FYADHPFIFlV

Chain	Residue	Details
A	PHE382-VAL392

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