5MA7

Structure of thermolysin in complex with inhibitor (JC306).

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	4
Details	binding site for residue ZN E 401

Chain	Residue
E	HIS142
E	HIS146
E	GLU166
E	7K0412

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

Chain	Residue
E	HOH586
E	ASP138
E	GLU177
E	ASP185
E	GLU187
E	GLU190

---

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

Chain	Residue
E	ASP57
E	ASP59
E	GLN61
E	HOH564
E	HOH574
E	HOH773

---

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

Chain	Residue
E	GLU177
E	ASN183
E	ASP185
E	GLU190
E	HOH573
E	HOH612

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

Chain	Residue
E	TYR193
E	THR194
E	ILE197
E	ASP200
E	HOH553
E	HOH758

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site_id	AC6
Number of Residues	9
Details	binding site for residue GOL E 406

Chain	Residue
E	PHE114
E	TRP115
E	GLU143
E	HIS146
E	TYR157
E	7K0412
E	HOH509
E	HOH520
E	HOH730

---

site_id	AC7
Number of Residues	7
Details	binding site for residue GOL E 407

Chain	Residue
E	GLY109
E	TYR110
E	ASN111
E	ASN112
E	HOH662
E	HOH692
E	HOH709

---

site_id	AC8
Number of Residues	6
Details	binding site for residue DMS E 408

Chain	Residue
E	TYR66
E	HIS216
E	SER218
E	TYR251
E	HOH609
E	HOH845

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site_id	AC9
Number of Residues	5
Details	binding site for residue DMS E 409

Chain	Residue
E	GLY95
E	PRO184
E	TRP186
E	HOH698
E	HOH724

---

site_id	AD1
Number of Residues	3
Details	binding site for residue DMS E 410

Chain	Residue
E	THR2
E	GLY3
E	ASN33

---

site_id	AD2
Number of Residues	6
Details	binding site for residue DMS E 411

Chain	Residue
E	GLY3
E	THR4
E	TYR28
E	ASP59
E	ASN60
E	HOH647

---

site_id	AD3
Number of Residues	20
Details	binding site for residue 7K0 E 412

Chain	Residue
E	TYR106
E	ASN111
E	ASN112
E	ALA113
E	PHE114
E	TRP115
E	VAL139
E	HIS142
E	GLU143
E	HIS146
E	TYR157
E	GLU166
E	LEU202
E	ARG203
E	HIS231
E	ZN401
E	GOL406
E	HOH501
E	HOH516
E	HOH542

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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

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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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