3T2H

Tetragonal thermolysin in the presence of TMAO

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	7
Details	BINDING SITE FOR RESIDUE CA E 317

Chain	Residue
E	ASP138
E	GLU177
E	ASP185
E	GLU187
E	GLU190
E	CA318
E	HOH361

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA E 318

Chain	Residue
E	ASP185
E	GLU190
E	CA317
E	HOH368
E	HOH413
E	GLU177
E	ASN183

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 319

Chain	Residue
E	ASP57
E	ASP59
E	GLN61
E	HOH399
E	HOH419
E	HOH424

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 320

Chain	Residue
E	TYR193
E	THR194
E	ILE197
E	ASP200
E	HOH369
E	HOH418

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 321

Chain	Residue
E	HIS142
E	HIS146
E	GLU166
E	CL329

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 322

Chain	Residue
E	HIS250
E	CL323
E	CL324
E	CL325

---

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL E 323

Chain	Residue
E	HIS250
E	ZN322

---

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CL E 329

Chain	Residue
E	HIS142
E	GLU143
E	HIS146
E	TYR157
E	GLU166
E	HIS231
E	ZN321
E	HOH471

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL E 324

Chain	Residue
E	ARG47
E	LYS239
E	THR249
E	HIS250
E	ZN322

---

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL E 328

Chain	Residue
E	GLY12
E	VAL13
E	LEU14
E	GLY15
E	ASP16
E	LYS18

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL E 325

Chain	Residue
E	LYS45
E	ARG47
E	HIS250
E	TYR251
E	ZN322

---

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL E 327

Chain	Residue
E	ARG285
E	HOH495

---

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL E 326

Chain	Residue
E	SER65

---

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL E 330

Chain	Residue
E	LEU54
E	HOH395
E	HOH630

---

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA E 331

Chain	Residue
E	TYR211
E	HOH431
E	HOH477
E	HOH496
E	HOH497
E	HOH669

---

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE TMO E 2001

Chain	Residue
E	ILE1
E	TYR29
E	ALA209
E	LYS210
E	GLY212
E	HOH498

---

site_id	BC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TMO E 2002

Chain	Residue
E	SER206
E	ASP207

---

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TMO E 2003

Chain	Residue
E	TRP115
E	GLU143

---

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMS E 2011

Chain	Residue
E	TYR66
E	HIS216
E	TYR251
E	HOH587

---

site_id	CC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS E 2012

Chain	Residue
E	TYR151
E	TYR242
E	HOH777

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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

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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
E	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
E	HIS231

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING:

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

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 176

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

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