1P12

CRYSTAL STRUCTURES OF ALPHA-LYTIC PROTEASE COMPLEXES WITH IRREVERSIBLY BOUND PHOSPHONATE ESTERS

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 E 1

Chain	Residue
E	ALA15
E	ASN15
E	ARG230
E	PRO233
E	HOH268
E	HOH279
E	HOH368
E	HOH382

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site_id	AC2
Number of Residues	24
Details	BINDING SITE FOR CHAIN I OF PHOSPHONATE ESTER INHIBITOR

Chain	Residue
E	LEU41
E	CYS42
E	HIS57
E	ARG125
E	THR128
E	TYR171
E	GLU174
E	GLY192
E	ARG192
E	GLY193
E	ASP194
E	SER195
E	GLN208
E	SER214
E	GLY215
E	GLY216
E	VAL217
E	HOH340
E	HOH349
E	HOH384
I	HOH143
I	HOH146
I	HOH175
E	SER40

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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
E	VAL53-CYS58

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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
E	CYS191-ILE200

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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
E	ASP102
E	SER195
E	GLY193
E	HIS57
E	SER214

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

Chain	Residue	Details
E	ASP102
E	SER195
E	GLY193
E	HIS57

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 609

Chain

Residue

Details

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