1TEC

CRYSTALLOGRAPHIC REFINEMENT BY INCORPORATION OF MOLECULAR DYNAMICS. THE THERMOSTABLE SERINE PROTEASE THERMITASE COMPLEXED WITH EGLIN-C

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0004252	molecular_function	serine-type endopeptidase activity
E	0005576	cellular_component	extracellular region
E	0005615	cellular_component	extracellular space
E	0006508	biological_process	proteolysis
E	0008236	molecular_function	serine-type peptidase activity
E	0019538	biological_process	protein metabolic process
E	0046872	molecular_function	metal ion binding
I	0004867	molecular_function	serine-type endopeptidase inhibitor activity
I	0009611	biological_process	response to wounding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 343

Chain	Residue
E	ASP5
E	ASP47
E	VAL82
E	ASN85
E	THR87
E	ILE89

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 344

Chain	Residue
E	THR64
E	GLN66
E	ASP57
E	ASP60
E	ASP62

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site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA E 345

Chain	Residue
E	ALA173
E	TYR175
E	ALA178
E	ASP201

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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. IAIVDTGVqsnH

Chain	Residue	Details
E	ILE34-HIS45

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

Chain	Residue	Details
E	HIS71-ALA81

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

Chain	Residue	Details
E	GLY223-GLY233

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site_id	PS00285
Number of Residues	12
Details	POTATO_INHIBITOR Potato inhibitor I family signature. FPEVVGktVdqA

Chain	Residue	Details
I	PHE10-ALA21

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	SITE: Reactive bond

Chain	Residue	Details
I	LEU45
E	HIS71
E	SER225

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site_id	SWS_FT_FI2
Number of Residues	11
Details	BINDING: BINDING => ECO:0000269|PubMed:1993669, ECO:0000269|PubMed:2688688, ECO:0007744|PDB:1TEC, ECO:0007744|PDB:3TEC

Chain	Residue	Details
E	ASP5
E	THR87
E	ILE89
E	ASP47
E	ASP57
E	ASP60
E	ASP62
E	THR64
E	GLN66
E	VAL82
E	ASN85

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:2688688, ECO:0007744|PDB:1TEC

Chain	Residue	Details
E	ALA173
E	TYR175
E	ALA178
E	ASP201

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:1993669, ECO:0007744|PDB:3TEC

Chain	Residue	Details
E	VAL199

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1sca

Chain	Residue	Details
E	ASP38
E	HIS71
E	SER225

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