5OX2

Crystal structure of thymoligase, a substrate-tailored peptiligase variant

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	3
Details	binding site for residue SO4 A 301

Chain	Residue
A	PRO172
A	SER173
A	ARG247

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site_id	AC2
Number of Residues	3
Details	binding site for residue SO4 A 302

Chain	Residue
A	LYS237
A	ALA274
A	GLN275

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site_id	AC3
Number of Residues	4
Details	binding site for residue SO4 A 303

Chain	Residue
A	SER260
A	LYS256
A	GLY258
A	ASP259

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site_id	AC4
Number of Residues	2
Details	binding site for residue SO4 A 304

Chain	Residue
A	THR158
A	GLY160

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Functional Information from PROSITE/UniProt

site_id	PS00136
Number of Residues	12
Details	SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDSGIdssH

Chain	Residue	Details
A	VAL28-HIS39

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site_id	PS00137
Number of Residues	11
Details	SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVLA

Chain	Residue	Details
A	HIS64-ALA74

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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":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"5249818","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	5
Details	Binding site: {}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues
Details	M-CSA 723

Chain	Residue	Details
A	ASP32	electrostatic interaction, electrostatic stabiliser
A	HIS64	proton acceptor, proton donor
A	ASN155	electrostatic interaction, electrostatic stabiliser
A	CYS221	nucleofuge, nucleophile, proton acceptor, proton donor

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