1PWV

Crystal structure of Anthrax Lethal Factor wild-type protein complexed with an optimised peptide substrate.

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	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
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
B	0003824	molecular_function	catalytic activity
B	0004222	molecular_function	metalloendopeptidase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0006508	biological_process	proteolysis
B	0008237	molecular_function	metallopeptidase activity
B	0008270	molecular_function	zinc ion binding
B	0030430	cellular_component	host cell cytoplasm
B	0035821	biological_process	modulation of process of another organism
B	0044164	cellular_component	host cell cytosol
B	0046872	molecular_function	metal ion binding
B	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	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01339, ECO:0000269|PubMed:19651869, ECO:0000269|PubMed:9573135

Chain	Residue	Details
A	GLU687
B	GLU687

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01339, ECO:0000269|PubMed:11700563, ECO:0000269|PubMed:14718924, ECO:0000269|PubMed:14718925, ECO:0000269|PubMed:15911756, ECO:0000269|PubMed:22342144, ECO:0000269|PubMed:25372673, ECO:0000269|PubMed:26492514, ECO:0000269|PubMed:26578066, ECO:0007744|PDB:1J7N, ECO:0007744|PDB:1PWP, ECO:0007744|PDB:1PWQ, ECO:0007744|PDB:1PWU, ECO:0007744|PDB:1PWW, ECO:0007744|PDB:1YQY, ECO:0007744|PDB:4DV8, ECO:0007744|PDB:4PKQ, ECO:0007744|PDB:4PKR, ECO:0007744|PDB:4PKS, ECO:0007744|PDB:4PKT, ECO:0007744|PDB:4PKV, ECO:0007744|PDB:4PKW, ECO:0007744|PDB:4WF6, ECO:0007744|PDB:4XM6, ECO:0007744|PDB:4XM7, ECO:0007744|PDB:5D1S, ECO:0007744|PDB:5D1T

Chain	Residue	Details
A	HIS686
A	HIS690
A	GLU735
B	HIS686
B	HIS690
B	GLU735

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01339

Chain	Residue	Details
A	TYR728
B	TYR728

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 11700563, 9573135, 1110468, 14697216, 14672720

Chain	Residue	Details
A	GLU687
A	TYR728

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site_id	CSA2
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 11700563, 9573135, 1110468, 14697216, 14672720

Chain	Residue	Details
B	GLU687
B	TYR728

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 641

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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site_id	MCSA2
Number of Residues	5
Details	M-CSA 641

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

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