5FSP

Structure of thermolysin prepared by the 'soak-and-freeze' method under 100 bar of krypton pressure

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	12
Details	BINDING SITE FOR RESIDUE VAL A 2318

Chain	Residue
A	ASN112
A	HOH2166
A	HOH2284
A	LYS2319
A	ALA113
A	GLU143
A	LEU202
A	ARG203
A	HIS231
A	KR1325
A	HOH2164
A	HOH2165

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE LYS A 2319

Chain	Residue
A	ASN111
A	ASN112
A	LEU202
A	HIS231
A	HOH2285
A	VAL2318

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 1317

Chain	Residue
A	HIS142
A	HIS146
A	GLU166
A	HOH2164
A	HOH2165
A	HOH2166

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE KR A 1318

Chain	Residue
A	TYR84
A	SER92
A	TYR93

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE KR A 1319

Chain	Residue
A	ARG35
A	GLY38
A	ALA98

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE KR A 1320

Chain	Residue
A	ASP191
A	VAL192
A	TYR193
A	PRO195

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE KR A 1321

Chain	Residue
A	GLU160
A	ARG220
A	ASN233
A	PHE281

---

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE KR A 1322

Chain	Residue
A	GLN119

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE KR A 1323

Chain	Residue
A	TYR27
A	GLY212
A	PRO214
A	HOH2212

---

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE KR A 1324

Chain	Residue
A	VAL7
A	ASN21
A	HOH2032

---

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE KR A 1325

Chain	Residue
A	HIS142
A	ARG203
A	VAL2318

---

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1326

Chain	Residue
A	TYR193
A	THR194
A	ILE197
A	ASP200
A	HOH2199
A	HOH2201

---

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1327

Chain	Residue
A	ASP57
A	ASP59
A	GLN61
A	HOH2087
A	HOH2088
A	HOH2090

---

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1328

Chain	Residue
A	ASP138
A	GLU177
A	ASP185
A	GLU187
A	GLU190
A	HOH2189

---

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 1329

Chain	Residue
A	GLU177
A	ASN183
A	ASP185
A	GLU190
A	HOH2192

---

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

---