4H57

Thermolysin inhibition

Replaces:  3FWD

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	HOH641

---

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

Chain	Residue
A	GLU190
A	HOH624
A	HOH642
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	HOH631
A	HOH634
A	HOH640

---

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	HOH574
A	HOH799

---

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

Chain	Residue
A	HIS142
A	HIS146
A	GLU166
A	0PJ406

---

site_id	AC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 0PJ A 406

Chain	Residue
A	TYR106
A	ASN111
A	ASN112
A	ALA113
A	PHE114
A	TRP115
A	HIS142
A	GLU143
A	HIS146
A	TYR157
A	GLU166
A	LEU202
A	ARG203
A	HIS231
A	ZN405
A	GOL407
A	DMS412
A	DMS412
A	HOH580
A	HOH665
A	HOH757

---

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	0PJ406
A	HOH524
A	HOH537
A	HOH556

---

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 408

Chain	Residue
A	GLY109
A	TYR110
A	ASN111
A	ASN112
A	GLN158
A	ASN227
A	HOH586
A	HOH630
A	HOH684
A	HOH810

---

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL A 409

Chain	Residue
A	GLY247
A	GLY248
A	VAL255
A	GLN273
A	TYR274
A	LEU275
A	HOH530
A	HOH581
A	HOH588
A	HOH612
A	HOH657

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMS A 410

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

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMS A 411

Chain	Residue
A	GLY95
A	PRO184
A	TRP186
A	HOH548
A	HOH732

---

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DMS A 412

Chain	Residue
A	TYR110
A	ASN112
A	PHE114
A	0PJ406
A	0PJ406
A	HOH579
A	HOH821

---

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS A 413

Chain	Residue
A	TYR66
A	TYR251
A	HOH583

---

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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