5N34

Thermolysin in complex with inhibitor JC276

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	8JQ412

---

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

Chain	Residue
E	HOH579
E	ASP138
E	GLU177
E	ASP185
E	GLU187
E	GLU190

---

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

Chain	Residue
E	ASP57
E	ASP59
E	GLN61
E	HOH574
E	HOH601
E	HOH760

---

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	HOH535
E	HOH587

---

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	HOH603
E	HOH738

---

site_id	AC6
Number of Residues	5
Details	binding site for residue DMS E 406

Chain	Residue
E	TYR66
E	HIS216
E	SER218
E	HOH830
E	HOH831

---

site_id	AC7
Number of Residues	3
Details	binding site for residue DMS E 407

Chain	Residue
E	THR2
E	GLY3
E	ASN33

---

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

Chain	Residue
E	GLY95
E	PRO184
E	TRP186
E	HOH563
E	HOH695

---

site_id	AC9
Number of Residues	4
Details	binding site for residue DMS E 409

Chain	Residue
E	GLY259
E	ARG260
E	ASP261
E	HOH521

---

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

Chain	Residue
E	TYR110
E	ASN227
E	8JQ412
E	HOH586

---

site_id	AD2
Number of Residues	6
Details	binding site for residue MPD E 411

Chain	Residue
E	GLN290
E	SER298
E	LYS307
E	HOH510
E	HOH734
E	HOH800

---

site_id	AD3
Number of Residues	16
Details	binding site for residue 8JQ E 412

Chain	Residue
E	ASN112
E	ALA113
E	ASN116
E	HIS142
E	GLU143
E	HIS146
E	TYR157
E	GLU166
E	ARG203
E	HIS231
E	ZN401
E	MPD410
E	HOH504
E	HOH543
E	HOH657
E	HOH726

---

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

---