8TLN

STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING CATALYSIS

Replaces:  3TLNReplaces:  1TLNReplaces:  2TLN

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 VAL E 1322

Chain	Residue
E	ASN112
E	ALA113
E	GLU143
E	ARG203
E	HIS231
E	HOH392
E	LYS1323

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE LYS E 1323

Chain	Residue
E	VAL1322
E	ASN111
E	ASN112

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site_id	AC3
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	HOH346

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 318

Chain	Residue
E	GLU177
E	ASN183
E	ASP185
E	GLU190
E	HOH353
E	HOH475

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site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 319

Chain	Residue
E	ASP57
E	ASP59
E	GLN61
E	HOH419
E	HOH482
E	HOH503

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site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 320

Chain	Residue
E	TYR193
E	THR194
E	ILE197
E	ASP200
E	HOH354
E	HOH480

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site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 321

Chain	Residue
E	HIS142
E	HIS146
E	GLU166
E	HOH392

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site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMS E 324

Chain	Residue
E	TYR66
E	SER218
E	TYR251
E	HOH506

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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	3
Details	BINDING:

Chain	Residue	Details
E	VAL289
E	SER291
E	THR293

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues
Details	M-CSA 176

Chain

Residue

Details

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