6QF2

X-Ray structure of Thermolysin crystallized on a silicon chip

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	5
Details	binding site for residue ZN A 401

Chain	Residue
A	HIS142
A	HIS146
A	GLU166
A	ZN408
A	HOH531

---

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

Chain	Residue
A	GLU190
A	HOH618
A	ASP138
A	GLU177
A	ASP185
A	GLU187

---

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

Chain	Residue
A	GLU177
A	ASN183
A	ASP185
A	GLU190
A	HOH549
A	HOH639

---

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

Chain	Residue
A	ASP57
A	ASP59
A	GLN61
A	HOH581
A	HOH632
A	HOH829

---

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

Chain	Residue
A	TYR193
A	THR194
A	ILE197
A	ASP200
A	HOH544
A	HOH800

---

site_id	AC6
Number of Residues	10
Details	binding site for residue LEU A 406

Chain	Residue
A	ASN112
A	ALA113
A	VAL139
A	GLU143
A	LEU202
A	ARG203
A	HIS231
A	LYS407
A	HOH531
A	HOH635

---

site_id	AC7
Number of Residues	7
Details	binding site for residue LYS A 407

Chain	Residue
A	ASN111
A	ASN112
A	PHE130
A	HIS231
A	LEU406
A	HOH635
A	HOH710

---

site_id	AC8
Number of Residues	6
Details	binding site for residue ZN A 408

Chain	Residue
A	TYR157
A	GLU166
A	HIS231
A	ZN401
A	HOH531
A	HOH635

---

site_id	AC9
Number of Residues	7
Details	binding site for residue NA A 409

Chain	Residue
A	TYR211
A	HOH523
A	HOH562
A	HOH629
A	HOH697
A	HOH805
A	HOH923

---

site_id	AD1
Number of Residues	7
Details	binding site for residue EDO A 410

Chain	Residue
A	GLY248
A	VAL255
A	VAL256
A	GLN273
A	LEU275
A	HOH568
A	HOH569

---

site_id	AD2
Number of Residues	6
Details	binding site for residue EDO A 411

Chain	Residue
A	ASN96
A	ASP185
A	GLU187
A	GLU190
A	GLY199
A	HOH598

---

site_id	AD3
Number of Residues	1
Details	binding site for residue EDO A 412

Chain	Residue
A	THR299

---

site_id	AD4
Number of Residues	4
Details	binding site for residue EDO A 413

Chain	Residue
A	GLY259
A	ARG260
A	ASP261
A	HOH695

---

site_id	AD5
Number of Residues	5
Details	binding site for residue EDO A 414

Chain	Residue
A	TYR274
A	ALA286
A	ALA287
A	HOH612
A	HOH617

---

site_id	AD6
Number of Residues	6
Details	binding site for residue EDO A 415

Chain	Residue
A	TYR217
A	SER282
A	GLY314
A	VAL315
A	LYS316
A	HOH650

---

site_id	AD7
Number of Residues	4
Details	binding site for residue EDO A 416

Chain	Residue
A	ILE1
A	THR2
A	GLY3
A	ASN33

---

site_id	AD8
Number of Residues	3
Details	binding site for residue EDO A 417

Chain	Residue
A	ILE1
A	LYS210
A	GLY212

---

site_id	AD9
Number of Residues	12
Details	binding site for residue PE5 A 418

Chain	Residue
A	TYR296
A	TYR296
A	GLY297
A	GLY297
A	HOH591
A	HOH591
A	HOH643
A	HOH643
A	THR293
A	THR293
A	ASP294
A	ASP294

---

site_id	AE1
Number of Residues	9
Details	binding site for residue PEG A 419

Chain	Residue
A	VAL13
A	SER65
A	PRO69
A	HIS105
A	HOH522
A	HOH597
A	HOH713
A	HOH841
A	HOH886

---

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

---