1AU9

SUBTILISIN BPN' MUTANT 8324 IN CITRATE

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	169
Number of Residues	1
Details	MUTATION FROM GLY TO ALA AT RESIDUE 169.

Chain	Residue
A	ALA169

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site_id	206
Number of Residues	1
Details	MUTATION FROM GLN TO CYS AT RESIDUE 206. AN UNKNOWN THIO CONTAINING MOIETY IS BOUND TO CYS 206.

Chain	Residue
A	CYS206

---

site_id	217
Number of Residues	1
Details	MUTATION FROM TYR TO LYS AT RESIDUE 217.

Chain	Residue
A	LYS217

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site_id	218
Number of Residues	1
Details	MUTATION FROM ASN TO SER AT RESIDUE 218.

Chain	Residue
A	SER218

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site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 295

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

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CA A 296

Chain	Residue
A	ALA169
A	TYR171
A	VAL174
A	GLU195
A	ASP197
A	HOH300
A	HOH340
A	HOH372

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE UNX A 277

Chain	Residue
A	CYS206
A	GLY215
A	UNX278

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE UNX A 278

Chain	Residue
A	CYS206
A	UNX277

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA A 290

Chain	Residue
A	SER37
A	VAL44
A	PHE58
A	ARG186

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IPA A 291

Chain	Residue
A	SER145
A	PHE189
A	HOH364

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site_id	C22
Number of Residues	1
Details	MUTATION FROM THR TO CYS AT RESIDUE 22. CYS 22 FORMS A DISULFIDE BOND WITH CYS 87.

Chain	Residue
A	CYS22

---

site_id	C87
Number of Residues	1
Details	MUTATION FROM SER TO CYS AT RESIDUE 87. CYS 87 FORMS A DISULFIDE BOND WITH CYS 22.

Chain	Residue
A	CYS87

---

site_id	CA1
Number of Residues	1
Details	HIGH AFFINITY CALCIUM BINDING SITE.

Chain	Residue
A	CA295

---

site_id	CA2
Number of Residues	1
Details	LOW AFFINITY CALCIUM BINDING SITE.

Chain	Residue
A	CA296

---

site_id	F50
Number of Residues	1
Details	MUTATION FROM MET TO PHE AT RESIDUE 50.

Chain	Residue
A	PHE50

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL28-HIS39

---

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

Chain	Residue	Details
A	HIS64-ALA74

---

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

Chain	Residue	Details
A	GLY219-GLY229

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	269
Details	Domain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
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

---

site_id	SWS_FT_FI3
Number of Residues	9
Details	Binding site: {}

Chain

Residue

Details

---

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

---

site_id	MCSA1
Number of Residues	4
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	SER221	nucleofuge, nucleophile, proton acceptor, proton donor

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