1SBN

REFINED CRYSTAL STRUCTURES OF SUBTILISIN NOVO IN COMPLEX WITH WILD-TYPE AND TWO MUTANT EGLINS. COMPARISON WITH OTHER SERINE PROTEINASE INHIBITOR COMPLEXES

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0004252	molecular_function	serine-type endopeptidase activity
E	0006508	biological_process	proteolysis
E	0008236	molecular_function	serine-type peptidase activity
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	8
Details	BINDING SITE FOR RESIDUE CA E 276

Chain	Residue
E	GLY169
E	LYS170
E	TYR171
E	VAL174
E	ALA176
E	GLU195
E	ASP197
E	HOH366

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 277

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

---

site_id	BLI
Number of Residues	8
Details	BINDING LOOP OF THE INHIBITOR EGLIN C

Chain	Residue
I	PRO42
I	VAL43
I	THR44
I	ARG45
I	ASP46
I	LEU47
I	ARG48
I	TYR49

---

site_id	CA1
Number of Residues	7
Details	CALCIUM BINDING SITE 1

Chain	Residue
E	GLY169
E	TYR171
E	VAL174
E	GLU195
E	ASP197
E	CA276
E	HOH366

---

site_id	CA2
Number of Residues	7
Details	CALCIUM BINDING SITE 2

Chain	Residue
E	GLN2
E	ASP41
E	LEU75
E	ASN77
E	ILE79
E	VAL81
E	CA277

---

site_id	CAT
Number of Residues	3
Details	CATALYTIC TRIAD OF ENZYME SUBTILISIN

Chain	Residue
E	ASP32
E	HIS64
E	SER221

---

site_id	S1
Number of Residues	8
Details	SUBSTRATE BINDING SITE 1

Chain	Residue
E	SER125
E	LEU126
E	GLY127
E	GLY128
E	ALA152
E	GLY154
E	ASN155
E	THR220

---

site_id	S1'
Number of Residues	6
Details	SUBSTRATE BINDING SITE 1'

Chain	Residue
E	HIS64
E	ASN155
E	ASN218
E	GLY219
E	SER221
E	MET222

---

site_id	S2
Number of Residues	4
Details	SUBSTRATE BINDING SITE 2

Chain	Residue
E	HIS64
E	LEU96
E	GLY100
E	SER125

---

site_id	S2'
Number of Residues	2
Details	SUBSTRATE BINDING SITE 2'

Chain	Residue
E	PHE189
E	ASN218

---

site_id	S3
Number of Residues	4
Details	SUBSTRATE BINDING SITE 3

Chain	Residue
E	SER101
E	LEU126
E	GLY127
E	GLY100

---

site_id	S3'
Number of Residues	3
Details	SUBSTRATE BINDING SITE 3'

Chain	Residue
E	ASN62
E	SER63
E	TYR217

---

site_id	S4
Number of Residues	5
Details	SUBSTRATE BINDING SITE 4

Chain	Residue
E	SER101
E	GLY102
E	TYR104
E	ILE107
E	GLY127

---

site_id	S4'
Number of Residues	1
Details	SUBSTRATE BINDING SITE 4'

Chain	Residue
E	ASN218

---

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
E	VAL28-HIS39

---

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

Chain	Residue	Details
E	HIS64-ALA74

---

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

Chain	Residue	Details
E	GLY219-GLY229

---

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

Chain	Residue	Details
I	PHE10-ALA21

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	SITE: Reactive bond

Chain	Residue	Details
I	ARG45
E	HIS64
E	SER221

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	BINDING:

Chain	Residue	Details
E	GLN2
E	ASP41
E	LEU75
E	ASN77
E	ILE79
E	VAL81
E	GLY169
E	TYR171
E	VAL174

---

Catalytic Information from CSA

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

Chain	Residue	Details
E	SER221
E	HIS64
E	ASP32

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 723

Chain	Residue	Details
E	ASP32	electrostatic interaction, electrostatic stabiliser
E	HIS64	proton acceptor, proton donor
E	ASN155	electrostatic interaction, electrostatic stabiliser
E	SER221	nucleofuge, nucleophile, proton acceptor, proton donor

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