5N3V

Thermolysin in complex with inhibitor JC292

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0004222	molecular_function	metalloendopeptidase activity
E	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN E 401

Chain	Residue
E	HIS142
E	HIS146
E	GLU166
E	8L5406

---

site_id	AC2
Number of Residues	6
Details	binding site for residue CA E 402

Chain	Residue
E	HOH766
E	ASP57
E	ASP59
E	GLN61
E	HOH585
E	HOH603

---

site_id	AC3
Number of Residues	6
Details	binding site for residue CA E 403

Chain	Residue
E	ASP138
E	GLU177
E	ASP185
E	GLU187
E	GLU190
E	HOH594

---

site_id	AC4
Number of Residues	6
Details	binding site for residue CA E 404

Chain	Residue
E	GLU177
E	ASN183
E	ASP185
E	GLU190
E	HOH547
E	HOH565

---

site_id	AC5
Number of Residues	6
Details	binding site for residue CA E 405

Chain	Residue
E	TYR193
E	THR194
E	ILE197
E	ASP200
E	HOH607
E	HOH741

---

site_id	AC6
Number of Residues	19
Details	binding site for residue 8L5 E 406

Chain	Residue
E	ASN112
E	ALA113
E	ASN116
E	HIS142
E	GLU143
E	HIS146
E	TYR157
E	GLU166
E	LEU202
E	ARG203
E	HIS231
E	ZN401
E	MPD407
E	HOH569
E	HOH590
E	HOH592
E	HOH678
E	HOH701
E	HOH734

---

site_id	AC7
Number of Residues	6
Details	binding site for residue MPD E 407

Chain	Residue
E	TYR110
E	ASN227
E	8L5406
E	HOH537
E	HOH702
E	HOH835

---

site_id	AC8
Number of Residues	5
Details	binding site for residue MPD E 408

Chain	Residue
E	GLN290
E	THR293
E	HOH633
E	HOH804
E	HOH829

---

site_id	AC9
Number of Residues	5
Details	binding site for residue DMS E 409

Chain	Residue
E	TYR66
E	HIS216
E	SER218
E	HOH782
E	HOH849

---

site_id	AD1
Number of Residues	4
Details	binding site for residue DMS E 410

Chain	Residue
E	THR2
E	GLY3
E	GLN31
E	ASN33

---

site_id	AD2
Number of Residues	4
Details	binding site for residue DMS E 411

Chain	Residue
E	GLY259
E	ARG260
E	ASP261
E	HOH516

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
E	VAL139-VAL148

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4808703","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4808703","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 176

Chain

Residue

Details

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