1JKY

Crystal Structure of the Anthrax Lethal Factor (LF): Wild-type LF Complexed with the N-terminal Sequence of MAPKK2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004222	molecular_function	metalloendopeptidase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
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	0030430	cellular_component	host cell cytoplasm
A	0035821	biological_process	modulation of process of another organism
A	0044164	cellular_component	host cell cytosol
A	0046872	molecular_function	metal ion binding
A	0090729	molecular_function	toxin activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY683-VAL692

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	SITE: Cleavage; by anthrax lethal factor

Chain	Residue	Details
B	PRO10

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330

Chain	Residue	Details
B	MET1
A	HIS690
A	GLU735

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01339

Chain	Residue	Details
A	TYR728

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1pwv

Chain	Residue	Details
A	GLU687
A	TYR728

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site_id	MCSA1
Number of Residues
Details	M-CSA 282

Chain	Residue	Details
A	HIS686	metal ligand
A	GLU687	proton acceptor, proton donor
A	HIS690	metal ligand
A	TYR728	electrostatic stabiliser
A	GLU735	metal ligand

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