4KS6

Crystal structure of the catalytic domain of botulinum neurotoxin BoNT/A C134S mutant with covalent inhibitor that modifies Cys-165 causing disorder in 166-174 stretch

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 501

Chain	Residue
A	HIS223
A	HIS227
A	GLU262
B	DPP2

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 502

Chain	Residue
A	LYS375
A	ILE376
A	THR414

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 503

Chain	Residue
A	ASN402
A	PGO506
A	HOH764
A	ASP339
A	ASN400

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 504

Chain	Residue
A	PRO140
A	ASP141
A	LYS415
A	LEU416
A	ASN418

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 505

Chain	Residue
A	LYS6
A	GLN7
A	PHE8
A	THR92

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PGO A 506

Chain	Residue
A	ARG283
A	LEU284
A	TYR287
A	PHE338
A	ASP339
A	GOL503
A	HOH943

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 507

Chain	Residue
A	ASN383
A	MET411
A	ASN412
A	HOH774

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PGO A 508

Chain	Residue
A	ASN238
A	PHE282
A	TYR285
A	TYR286
A	HOH941

---

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO A 509

Chain	Residue
A	GLN139
A	HOH660

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 510

Chain	Residue
A	ILE160
A	PHE188
A	SER189
A	HOH904

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 511

Chain	Residue
A	LYS212
A	ARG283
A	ASP339
A	ASN405
A	GLU407
A	HOH872

---

site_id	BC3
Number of Residues	24
Details	BINDING SITE FOR CHAIN B OF PEPTIDE INHIBITOR MPT-DPP-DAR-G-DPN-NH2

Chain	Residue
A	PHE163
A	GLU164
A	CYS165
A	PHE194
A	THR215
A	HIS223
A	GLU224
A	HIS227
A	TYR251
A	LEU256
A	GLU262
A	ARG363
A	TYR366
A	ASN368
A	PHE369
A	ASP370
A	ZN501
A	HOH782
A	HOH804
A	HOH811
A	HOH824
A	HOH825
B	HOH101
B	HOH102

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095

Chain	Residue	Details
A	GLU224

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:17173035, ECO:0000305|PubMed:9783750, 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	HIS223
A	HIS227

---

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

---

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

---