3DDA

Crystal structure of the catalytic domain of Botulinum neurotoxin serotype a with a snap-25 peptide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004222	molecular_function	metalloendopeptidase activity
A	0006508	biological_process	proteolysis
A	0008270	molecular_function	zinc ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 450

Chain	Residue
A	HIS223
A	HIS227
A	GLU262
B	GLN197

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 451

Chain	Residue
A	LYS340
A	HOH536
A	HOH621
A	HOH820

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NH2 B 203

Chain	Residue
B	LYS201
B	MET202
A	ASP370

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	THR220-GLY229

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	SITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA) => ECO:0000269|PubMed:9886085, ECO:0000305|PubMed:15592454

Chain	Residue	Details
B	GLN197

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site_id	SWS_FT_FI2
Number of Residues	1
Details	SITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type C (BoNT/C) => ECO:0000269|PubMed:9886085, ECO:0000305|PubMed:15592454

Chain	Residue	Details
B	ARG198
A	HIS227

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:17173035, ECO:0007744|PDB:2NYY, ECO:0007744|PDB:2NZ9, ECO:0007744|PDB:3BTA, ECO:0007744|PDB:3QIX, ECO:0007744|PDB:3QIY, ECO:0007744|PDB:3QIZ, ECO:0007744|PDB:3QJ0

Chain	Residue	Details
A	GLU262

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site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000305|PubMed:11827515

Chain	Residue	Details
A	ARG363
A	TYR366

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1i1e

Chain	Residue	Details
A	GLU262
A	TYR366
A	ARG363

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