1NLU

Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0006508	biological_process	proteolysis
A	0008236	molecular_function	serine-type peptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 501

Chain	Residue
A	ASP328
A	VAL329
A	GLY344
A	GLY346
A	ASP348
A	HOH502

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site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR CHAIN B OF PSEUDO-IODOTYROSTATIN

Chain	Residue
A	SER133
A	LEU134
A	GLY135
A	TRP136
A	GLY169
A	ASP170
A	GLU171
A	GLU175
A	ARG179
A	SER190
A	GLY285
A	THR286
A	SER287
A	HOH736
B	HOH182
A	ASP74
A	GLU80
A	TRP81

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site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR CHAIN C OF PSEUDO-IODOTYROSTATIN

Chain	Residue
A	GLY79
A	GLU80
A	GLU222
A	TRP231
A	GLN268
A	GLN281
A	ILE283
A	GLY284
A	HOH908
C	HOH152
C	HOH288
C	HOH360
C	HOH380
C	HOH442

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Functional Information from PROSITE/UniProt

site_id	PS00138
Number of Residues	11
Details	SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSlAsPiFVG

Chain	Residue	Details
A	GLY285-GLY295

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	364
Details	Domain: {"description":"Peptidase S53","evidences":[{"source":"PROSITE-ProRule","id":"PRU01032","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	19
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	3
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"11323721","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11747435","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11323721","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11747435","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GA4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GA6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NLU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6M8W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6M8Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6M9C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6M9D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6M9F","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 12673349, 1562589, 10488127

Chain	Residue	Details
A	GLU80
A	ASP170
A	SER287
A	ASP84

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site_id	MCSA1
Number of Residues	4
Details	M-CSA 380

Chain	Residue	Details
A	GLU80	proton shuttle (general acid/base)
A	ASP84	proton shuttle (general acid/base)
A	ASP170	electrostatic stabiliser
A	SER287	covalent catalysis

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