2TMN

CRYSTALLOGRAPHIC STRUCTURAL ANALYSIS OF PHOSPHORAMIDATES AS INHIBITORS AND TRANSITION-STATE ANALOGS OF THERMOLYSIN

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	6
Details	BINDING SITE FOR RESIDUE CA E 317

Chain	Residue
E	ASP138
E	GLU177
E	ASP185
E	GLU187
E	GLU190
E	HOH338

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

Chain	Residue
E	GLU190
E	HOH345
E	HOH431
E	GLU177
E	ASN183
E	ASP185

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

Chain	Residue
E	ASP57
E	ASP59
E	GLN61
E	HOH394
E	HOH438
E	HOH454

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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	HOH346
E	HOH436

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site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN E 321

Chain	Residue
E	HIS142
E	HIS146
E	TYR157
E	GLU166
E	0FA322

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site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 0FA E 322

Chain	Residue
E	ASN112
E	ALA113
E	HIS142
E	GLU143
E	HIS146
E	TYR157
E	GLU166
E	LEU202
E	ARG203
E	HIS231
E	ZN321
E	HOH353
E	HOH380
E	HOH490
E	HOH491

---

site_id	S1
Number of Residues	1
Details	ACTIVE SITE SUBSITE S1

Chain	Residue
E	PHE114

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site_id	S1P
Number of Residues	7
Details	ACTIVE SITE SUBSITE S1 PRIME

Chain	Residue
E	PHE130
E	LEU133
E	VAL139
E	ILE188
E	GLY189
E	VAL192
E	LEU202

---

site_id	S2
Number of Residues	1
Details	ACTIVE SITE SUBSITE S2

Chain	Residue
E	TRP115

---

site_id	S2P
Number of Residues	2
Details	ACTIVE SITE SUBSITE S2 PRIME

Chain	Residue
E	PHE130
E	LEU202

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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

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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

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1tlp

Chain	Residue	Details
E	HIS231
E	GLU143

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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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