1SPB

SUBTILISIN BPN' PROSEGMENT (77 RESIDUES) COMPLEXED WITH A MUTANT SUBTILISIN BPN' (266 RESIDUES). CRYSTAL PH 4.6. CRYSTALLIZATION TEMPERATURE 20 C DIFFRACTION TEMPERATURE-160 C

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA S 297

Chain	Residue
S	GLY169
S	TYR171
S	VAL174
S	GLU195
S	ASP197
S	HOH304

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
S	HIS64-ALA74

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:5249818

Chain	Residue	Details
S	ASN32
S	HIS64
S	ALA230

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site_id	SWS_FT_FI2
Number of Residues	9
Details	BINDING:

Chain	Residue	Details
S	GLN2
S	ASP41
S	VAL84
S	PRO86
S	ALA88
S	LEU90
S	GLY178
S	VAL180
S	SER183

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 723

Chain	Residue	Details
S	ASN32	electrostatic interaction, electrostatic stabiliser
S	HIS64	proton acceptor, proton donor
S	THR164	electrostatic interaction, electrostatic stabiliser
S	ALA230	nucleofuge, nucleophile, proton acceptor, proton donor

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