3QGO

Structure of Thermolysin in complex with L-Phenylalanine methylester

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	6
Details	BINDING SITE FOR RESIDUE CA A 401

Chain	Residue
A	ASP138
A	GLU177
A	ASP185
A	GLU187
A	GLU190
A	HOH465

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 402

Chain	Residue
A	GLU190
A	HOH493
A	HOH502
A	GLU177
A	ASN183
A	ASP185

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 403

Chain	Residue
A	ASP57
A	ASP59
A	GLN61
A	HOH462
A	HOH470
A	HOH471

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 404

Chain	Residue
A	TYR193
A	THR194
A	ILE197
A	ASP200
A	HOH510
A	HOH524

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 405

Chain	Residue
A	HIS142
A	GLU143
A	HIS146
A	GLU166

---

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 0A9 A 406

Chain	Residue
A	ASN112
A	ALA113
A	VAL139
A	GLU143
A	ILE188
A	LEU202
A	ARG203
A	HIS231
A	HOH354
A	HOH633

---

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 0A9 A 407

Chain	Residue
A	THR26
A	TYR29
A	TYR211
A	GLY212
A	ASP213
A	HOH394
A	0A9408
A	HOH642

---

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 0A9 A 408

Chain	Residue
A	ILE1
A	SER25
A	TYR29
A	TYR211
A	GLY212
A	HOH360
A	0A9407
A	HOH655
A	HOH745

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMS A 317

Chain	Residue
A	TYR66
A	HIS216
A	SER218
A	HOH558
A	HOH660

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMS A 318

Chain	Residue
A	ILE1
A	THR2
A	GLY3
A	GLN31
A	ASN33

---

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT A 1428

Chain	Residue
A	TYR24
A	TYR24
A	SER25

---

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE P6G A 319

Chain	Residue
A	THR293
A	ASP294
A	TYR296
A	GLY297
A	GLY297
A	HOH361
A	HOH361
A	HOH570
A	HOH570

---

site_id	BC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE P6G A 320

Chain	Residue
A	PHE178
A	TRP186
A	SER245
A	GLN246
A	GLY257
A	GLY259
A	ARG260
A	ASP261
A	GLN273
A	HOH457
A	HOH489
A	HOH609
A	HOH670
A	HOH766

---

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	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703

Chain	Residue	Details
A	GLU143

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703

Chain	Residue	Details
A	HIS231

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING:

Chain	Residue	Details
A	ASP57
A	ASP185
A	GLU187
A	GLU190
A	TYR193
A	THR194
A	ILE197
A	ASP200
A	ASP59
A	GLN61
A	ASP138
A	HIS142
A	HIS146
A	GLU166
A	GLU177
A	ASN183

---

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

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