1BOQ

PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRITICAL IN CATALYZING THE FOLDING OF ALPHA-LYTIC PROTEASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 199

Chain	Residue
A	HIS36
A	ARG89
A	ARG140
A	GLY141
A	SER143
A	HOH225

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site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 200

Chain	Residue
A	PRO186
A	HOH231
A	HOH258
A	HOH304
A	HOH318
A	ALA1
A	ASN2
A	ARG183

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Functional Information from PROSITE/UniProt

site_id	PS00134
Number of Residues	6
Details	TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAGHC

Chain	Residue	Details
A	VAL32-CYS37

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site_id	PS00135
Number of Residues	12
Details	TRYPSIN_SER Serine proteases, trypsin family, serine active site. CMgrGDSGGSWI

Chain	Residue	Details
A	CYS137-ILE148

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1ssx

Chain	Residue	Details
A	SER143
A	GLY141
A	ASP63
A	HIS36
A	SER159

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site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1ssx

Chain	Residue	Details
A	SER143
A	GLY141
A	ASP63
A	HIS36

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 609

Chain	Residue	Details
A	HIS36	proton acceptor, proton donor
A	ASP63	electrostatic stabiliser
A	GLY141	electrostatic stabiliser
A	SER143	electrostatic stabiliser
A	SER159	electrostatic stabiliser

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