3QH5

Structure of Thermolysin in complex with N-Carbobenzyloxy-L-aspartic acid and L-Phenylalanine Methyl Ester

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 317

Chain	Residue
A	ASP138
A	GLU177
A	ASP185
A	GLU187
A	GLU190
A	HOH331

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 318

Chain	Residue
A	GLU190
A	HOH489
A	HOH497
A	GLU177
A	ASN183
A	ASP185

---

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

Chain	Residue
A	ASP57
A	ASP59
A	GLN61
A	HOH337
A	HOH351
A	HOH359

---

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

Chain	Residue
A	TYR193
A	THR194
A	ILE197
A	ASP200
A	HOH347
A	HOH348

---

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

Chain	Residue
A	HIS142
A	HIS146
A	GLU166
A	NX6999

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 0A9 A 322

Chain	Residue
A	THR26
A	TYR27
A	TYR29
A	TYR211
A	GLY212
A	ASP213
A	0A9323
A	HOH528
A	HOH602

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 0A9 A 323

Chain	Residue
A	ILE1
A	SER25
A	TYR29
A	TYR211
A	GLY212
A	0A9322
A	HOH541

---

site_id	AC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE NX6 A 999

Chain	Residue
A	ASN112
A	ALA113
A	LEU133
A	VAL139
A	HIS142
A	GLU143
A	HIS146
A	TYR157
A	GLU166
A	ILE188
A	LEU202
A	HIS231
A	ZN321
A	HOH491
A	HOH567

---

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PG4 A 324

Chain	Residue
A	GLN246
A	GLY257
A	ILE258
A	GLY259
A	GLN273
A	HOH467
A	HOH565
A	HOH570

---

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PEG A 325

Chain	Residue
A	SER65
A	ALA68
A	PRO69
A	HIS105
A	ASP124
A	PRO132
A	HOH511
A	HOH571

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG A 326

Chain	Residue
A	TRP115
A	HIS146
A	TYR157
A	HOH366
A	HOH506

---

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG A 327

Chain	Residue
A	ILE1
A	ASN33
A	GLY36
A	ASN37
A	SER198

---

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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