1WSD

Alkaline M-protease form I crystal structure

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 276

Chain	Residue
A	GLN2
A	ASP41
A	LEU75
A	ASN77
A	ILE79
A	VAL81

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site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 277

Chain	Residue
A	VAL104
A	PRO210
A	HOH293
A	HOH328
A	HOH367
A	SER37
A	GLN59
A	SER103

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Functional Information from PROSITE/UniProt

site_id	PS00136
Number of Residues	11
Details	SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGIst.H

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. HGThVAGtIAA

Chain	Residue	Details
A	HIS64-ALA74

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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
A	GLY219-GLY229

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240

Chain	Residue	Details
A	ARG145
A	ALA179

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:15299321, ECO:0007744|PDB:1MPT, ECO:0007744|PDB:1WSD

Chain	Residue	Details
A	GLY115
A	SER153
A	SER190
A	ALA194
A	LEU196

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:15299321, ECO:0007744|PDB:1WSD

Chain	Residue	Details
A	TYR192

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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
A	SER221
A	HIS64
A	ASP32

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