5M9W

Experimental MAD phased structure of thermolysin in complex with inhibitor JC65.

Functional Information from GO Data

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

Functional Information from PDB Data

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

Chain	Residue
A	HIS142
A	HIS146
A	GLU166
A	7GR412

---

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

Chain	Residue
A	HOH768
A	ASP57
A	ASP59
A	GLN61
A	HOH567
A	HOH578

---

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

Chain	Residue
A	TYR193
A	THR194
A	ILE197
A	ASP200
A	HOH588
A	HOH749

---

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

Chain	Residue
A	GLU177
A	ASN183
A	ASP185
A	GLU190
A	HOH540
A	HOH564

---

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

Chain	Residue
A	ASP138
A	GLU177
A	ASP185
A	GLU187
A	GLU190
A	HOH584

---

site_id	AC6
Number of Residues	7
Details	binding site for residue GOL A 406

Chain	Residue
A	GLY109
A	TYR110
A	ASN111
A	ASN112
A	GLN158
A	HOH563
A	HOH694

---

site_id	AC7
Number of Residues	8
Details	binding site for residue GOL A 407

Chain	Residue
A	PHE114
A	TRP115
A	HIS146
A	TYR157
A	7GR412
A	HOH512
A	HOH545
A	HOH649

---

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

Chain	Residue
A	TYR110
A	ASN112
A	PHE114
A	7GR412
A	7GR412

---

site_id	AC9
Number of Residues	3
Details	binding site for residue DMS A 409

Chain	Residue
A	THR2
A	GLY3
A	ASN33

---

site_id	AD1
Number of Residues	5
Details	binding site for residue DMS A 410

Chain	Residue
A	TYR66
A	HIS216
A	SER218
A	TYR251
A	HOH831

---

site_id	AD2
Number of Residues	7
Details	binding site for residue DMS A 411

Chain	Residue
A	GLY3
A	THR4
A	TYR28
A	ASP59
A	ASN60
A	HOH650
A	HOH753

---

site_id	AD3
Number of Residues	22
Details	binding site for residue 7GR A 412

Chain	Residue
A	TYR106
A	ASN111
A	ASN112
A	ALA113
A	PHE114
A	TRP115
A	PHE130
A	HIS142
A	GLU143
A	HIS146
A	TYR157
A	GLU166
A	LEU202
A	ARG203
A	HIS231
A	ZN401
A	GOL407
A	DMS408
A	DMS408
A	HOH502
A	HOH550
A	HOH576

---

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
A	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
A	HIS142	metal ligand
A	GLU143	electrostatic stabiliser, metal ligand
A	HIS146	metal ligand
A	TYR157	electrostatic stabiliser, hydrogen bond donor, steric role
A	GLU166	metal ligand
A	ASP226	activator, electrostatic stabiliser, hydrogen bond acceptor
A	HIS231	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

---