1SMP

CRYSTAL STRUCTURE OF A COMPLEX BETWEEN SERRATIA MARCESCENS METALLO-PROTEASE AND AN INHIBITOR FROM ERWINIA CHRYSANTHEMI

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001907	biological_process	symbiont-mediated killing of host cell
A	0004222	molecular_function	metalloendopeptidase activity
A	0005509	molecular_function	calcium ion binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0030198	biological_process	extracellular matrix organization
A	0030574	biological_process	collagen catabolic process
A	0031012	cellular_component	extracellular matrix
A	0035821	biological_process	modulation of process of another organism
A	0046872	molecular_function	metal ion binding
A	0090729	molecular_function	toxin activity
I	0004857	molecular_function	enzyme inhibitor activity
I	0004866	molecular_function	endopeptidase inhibitor activity
I	0008191	molecular_function	metalloendopeptidase inhibitor activity
I	0010951	biological_process	negative regulation of endopeptidase activity
I	0030414	molecular_function	peptidase inhibitor activity
I	0042597	cellular_component	periplasmic space

Functional Information from PDB Data

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TFTHEIGHAL

Chain	Residue	Details
A	THR173-LEU182

site_id	PS00330
Number of Residues	19
Details	HEMOLYSIN_CALCIUM Hemolysin-type calcium-binding region signature. DvLfgggGaDeLwGGagkD

Chain	Residue	Details
A	ASP356-ASP374

Functional Information from SwissProt/UniProt

Chain	Residue	Details
A	GLU177