5UGF

Crystal structure of human purine nucleoside phosphorylase (F159Y) mutant complexed with DADMe-ImmG and phosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000255	biological_process	allantoin metabolic process
A	0001882	molecular_function	nucleoside binding
A	0002060	molecular_function	purine nucleobase binding
A	0003824	molecular_function	catalytic activity
A	0004731	molecular_function	purine-nucleoside phosphorylase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006148	biological_process	inosine catabolic process
A	0006149	biological_process	deoxyinosine catabolic process
A	0006157	biological_process	deoxyadenosine catabolic process
A	0006166	biological_process	purine ribonucleoside salvage
A	0006204	biological_process	IMP catabolic process
A	0006738	biological_process	nicotinamide riboside catabolic process
A	0006955	biological_process	immune response
A	0009116	biological_process	nucleoside metabolic process
A	0009165	biological_process	nucleotide biosynthetic process
A	0009410	biological_process	response to xenobiotic stimulus
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0032743	biological_process	positive regulation of interleukin-2 production
A	0034418	biological_process	urate biosynthetic process
A	0034774	cellular_component	secretory granule lumen
A	0042102	biological_process	positive regulation of T cell proliferation
A	0042301	molecular_function	phosphate ion binding
A	0042802	molecular_function	identical protein binding
A	0043101	biological_process	purine-containing compound salvage
A	0046059	biological_process	dAMP catabolic process
A	0046638	biological_process	positive regulation of alpha-beta T cell differentiation
A	0047975	molecular_function	guanosine phosphorylase activity
A	0070062	cellular_component	extracellular exosome
A	1904813	cellular_component	ficolin-1-rich granule lumen
B	0000255	biological_process	allantoin metabolic process
B	0001882	molecular_function	nucleoside binding
B	0002060	molecular_function	purine nucleobase binding
B	0003824	molecular_function	catalytic activity
B	0004731	molecular_function	purine-nucleoside phosphorylase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0006148	biological_process	inosine catabolic process
B	0006149	biological_process	deoxyinosine catabolic process
B	0006157	biological_process	deoxyadenosine catabolic process
B	0006166	biological_process	purine ribonucleoside salvage
B	0006204	biological_process	IMP catabolic process
B	0006738	biological_process	nicotinamide riboside catabolic process
B	0006955	biological_process	immune response
B	0009116	biological_process	nucleoside metabolic process
B	0009165	biological_process	nucleotide biosynthetic process
B	0009410	biological_process	response to xenobiotic stimulus
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0016763	molecular_function	pentosyltransferase activity
B	0032743	biological_process	positive regulation of interleukin-2 production
B	0034418	biological_process	urate biosynthetic process
B	0034774	cellular_component	secretory granule lumen
B	0042102	biological_process	positive regulation of T cell proliferation
B	0042301	molecular_function	phosphate ion binding
B	0042802	molecular_function	identical protein binding
B	0043101	biological_process	purine-containing compound salvage
B	0046059	biological_process	dAMP catabolic process
B	0046638	biological_process	positive regulation of alpha-beta T cell differentiation
B	0047975	molecular_function	guanosine phosphorylase activity
B	0070062	cellular_component	extracellular exosome
B	1904813	cellular_component	ficolin-1-rich granule lumen
C	0000255	biological_process	allantoin metabolic process
C	0001882	molecular_function	nucleoside binding
C	0002060	molecular_function	purine nucleobase binding
C	0003824	molecular_function	catalytic activity
C	0004731	molecular_function	purine-nucleoside phosphorylase activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006139	biological_process	nucleobase-containing compound metabolic process
C	0006148	biological_process	inosine catabolic process
C	0006149	biological_process	deoxyinosine catabolic process
C	0006157	biological_process	deoxyadenosine catabolic process
C	0006166	biological_process	purine ribonucleoside salvage
C	0006204	biological_process	IMP catabolic process
C	0006738	biological_process	nicotinamide riboside catabolic process
C	0006955	biological_process	immune response
C	0009116	biological_process	nucleoside metabolic process
C	0009165	biological_process	nucleotide biosynthetic process
C	0009410	biological_process	response to xenobiotic stimulus
C	0016740	molecular_function	transferase activity
C	0016757	molecular_function	glycosyltransferase activity
C	0016763	molecular_function	pentosyltransferase activity
C	0032743	biological_process	positive regulation of interleukin-2 production
C	0034418	biological_process	urate biosynthetic process
C	0034774	cellular_component	secretory granule lumen
C	0042102	biological_process	positive regulation of T cell proliferation
C	0042301	molecular_function	phosphate ion binding
C	0042802	molecular_function	identical protein binding
C	0043101	biological_process	purine-containing compound salvage
C	0046059	biological_process	dAMP catabolic process
C	0046638	biological_process	positive regulation of alpha-beta T cell differentiation
C	0047975	molecular_function	guanosine phosphorylase activity
C	0070062	cellular_component	extracellular exosome
C	1904813	cellular_component	ficolin-1-rich granule lumen
D	0000255	biological_process	allantoin metabolic process
D	0001882	molecular_function	nucleoside binding
D	0002060	molecular_function	purine nucleobase binding
D	0003824	molecular_function	catalytic activity
D	0004731	molecular_function	purine-nucleoside phosphorylase activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006139	biological_process	nucleobase-containing compound metabolic process
D	0006148	biological_process	inosine catabolic process
D	0006149	biological_process	deoxyinosine catabolic process
D	0006157	biological_process	deoxyadenosine catabolic process
D	0006166	biological_process	purine ribonucleoside salvage
D	0006204	biological_process	IMP catabolic process
D	0006738	biological_process	nicotinamide riboside catabolic process
D	0006955	biological_process	immune response
D	0009116	biological_process	nucleoside metabolic process
D	0009165	biological_process	nucleotide biosynthetic process
D	0009410	biological_process	response to xenobiotic stimulus
D	0016740	molecular_function	transferase activity
D	0016757	molecular_function	glycosyltransferase activity
D	0016763	molecular_function	pentosyltransferase activity
D	0032743	biological_process	positive regulation of interleukin-2 production
D	0034418	biological_process	urate biosynthetic process
D	0034774	cellular_component	secretory granule lumen
D	0042102	biological_process	positive regulation of T cell proliferation
D	0042301	molecular_function	phosphate ion binding
D	0042802	molecular_function	identical protein binding
D	0043101	biological_process	purine-containing compound salvage
D	0046059	biological_process	dAMP catabolic process
D	0046638	biological_process	positive regulation of alpha-beta T cell differentiation
D	0047975	molecular_function	guanosine phosphorylase activity
D	0070062	cellular_component	extracellular exosome
D	1904813	cellular_component	ficolin-1-rich granule lumen
E	0000255	biological_process	allantoin metabolic process
E	0001882	molecular_function	nucleoside binding
E	0002060	molecular_function	purine nucleobase binding
E	0003824	molecular_function	catalytic activity
E	0004731	molecular_function	purine-nucleoside phosphorylase activity
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006139	biological_process	nucleobase-containing compound metabolic process
E	0006148	biological_process	inosine catabolic process
E	0006149	biological_process	deoxyinosine catabolic process
E	0006157	biological_process	deoxyadenosine catabolic process
E	0006166	biological_process	purine ribonucleoside salvage
E	0006204	biological_process	IMP catabolic process
E	0006738	biological_process	nicotinamide riboside catabolic process
E	0006955	biological_process	immune response
E	0009116	biological_process	nucleoside metabolic process
E	0009165	biological_process	nucleotide biosynthetic process
E	0009410	biological_process	response to xenobiotic stimulus
E	0016740	molecular_function	transferase activity
E	0016757	molecular_function	glycosyltransferase activity
E	0016763	molecular_function	pentosyltransferase activity
E	0032743	biological_process	positive regulation of interleukin-2 production
E	0034418	biological_process	urate biosynthetic process
E	0034774	cellular_component	secretory granule lumen
E	0042102	biological_process	positive regulation of T cell proliferation
E	0042301	molecular_function	phosphate ion binding
E	0042802	molecular_function	identical protein binding
E	0043101	biological_process	purine-containing compound salvage
E	0046059	biological_process	dAMP catabolic process
E	0046638	biological_process	positive regulation of alpha-beta T cell differentiation
E	0047975	molecular_function	guanosine phosphorylase activity
E	0070062	cellular_component	extracellular exosome
E	1904813	cellular_component	ficolin-1-rich granule lumen
F	0000255	biological_process	allantoin metabolic process
F	0001882	molecular_function	nucleoside binding
F	0002060	molecular_function	purine nucleobase binding
F	0003824	molecular_function	catalytic activity
F	0004731	molecular_function	purine-nucleoside phosphorylase activity
F	0005515	molecular_function	protein binding
F	0005576	cellular_component	extracellular region
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006139	biological_process	nucleobase-containing compound metabolic process
F	0006148	biological_process	inosine catabolic process
F	0006149	biological_process	deoxyinosine catabolic process
F	0006157	biological_process	deoxyadenosine catabolic process
F	0006166	biological_process	purine ribonucleoside salvage
F	0006204	biological_process	IMP catabolic process
F	0006738	biological_process	nicotinamide riboside catabolic process
F	0006955	biological_process	immune response
F	0009116	biological_process	nucleoside metabolic process
F	0009165	biological_process	nucleotide biosynthetic process
F	0009410	biological_process	response to xenobiotic stimulus
F	0016740	molecular_function	transferase activity
F	0016757	molecular_function	glycosyltransferase activity
F	0016763	molecular_function	pentosyltransferase activity
F	0032743	biological_process	positive regulation of interleukin-2 production
F	0034418	biological_process	urate biosynthetic process
F	0034774	cellular_component	secretory granule lumen
F	0042102	biological_process	positive regulation of T cell proliferation
F	0042301	molecular_function	phosphate ion binding
F	0042802	molecular_function	identical protein binding
F	0043101	biological_process	purine-containing compound salvage
F	0046059	biological_process	dAMP catabolic process
F	0046638	biological_process	positive regulation of alpha-beta T cell differentiation
F	0047975	molecular_function	guanosine phosphorylase activity
F	0070062	cellular_component	extracellular exosome
F	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue PO4 A 301

Chain	Residue
A	GLY32
A	HOH411
A	HOH413
A	SER33
A	HIS64
A	ARG84
A	HIS86
A	ASN115
A	ALA116
A	SER220
A	IM5308

---

site_id	AC2
Number of Residues	4
Details	binding site for residue PO4 A 302

Chain	Residue
A	ARG148
C	PRO92
C	GLN144
C	HOH452

---

site_id	AC3
Number of Residues	6
Details	binding site for residue PO4 A 303

Chain	Residue
A	ASN151
A	ASP152
A	GLU153
A	ARG154
A	HOH403
A	HOH471

---

site_id	AC4
Number of Residues	4
Details	binding site for residue PO4 A 304

Chain	Residue
A	ARG133
A	HOH412
C	ARG207
C	TYR249

---

site_id	AC5
Number of Residues	4
Details	binding site for residue PO4 A 305

Chain	Residue
A	ARG207
A	TYR249
A	HOH420
B	ARG133

---

site_id	AC6
Number of Residues	5
Details	binding site for residue PO4 A 306

Chain	Residue
A	ARG133
A	ARG168
A	ARG171
A	GLU189
C	TYR249

---

site_id	AC7
Number of Residues	4
Details	binding site for residue PO4 A 307

Chain	Residue
A	ARG229
A	HOH410
A	HOH426
A	HOH456

---

site_id	AC8
Number of Residues	15
Details	binding site for residue IM5 A 308

Chain	Residue
A	TYR88
A	ALA116
A	GLY118
A	VAL195
A	PHE200
A	GLU201
A	VAL217
A	GLY218
A	MET219
A	THR242
A	ASN243
A	HIS257
A	PO4301
A	HOH460
B	TYR159

---

site_id	AC9
Number of Residues	11
Details	binding site for residue PO4 B 301

Chain	Residue
B	GLY32
B	SER33
B	HIS64
B	ARG84
B	HIS86
B	ASN115
B	ALA116
B	SER220
B	IM5306
B	HOH412
B	HOH416

---

site_id	AD1
Number of Residues	4
Details	binding site for residue PO4 B 302

Chain	Residue
A	PRO92
A	GLN144
B	MET1
B	ARG148

---

site_id	AD2
Number of Residues	3
Details	binding site for residue PO4 B 303

Chain	Residue
B	ARG207
B	HOH405
C	ARG133

---

site_id	AD3
Number of Residues	3
Details	binding site for residue PO4 B 304

Chain	Residue
B	THR43
B	GLN44
B	HOH476

---

site_id	AD4
Number of Residues	4
Details	binding site for residue PO4 B 305

Chain	Residue
B	THR6
B	TYR7
B	GLU8
B	ARG154

---

site_id	AD5
Number of Residues	17
Details	binding site for residue IM5 B 306

Chain	Residue
B	TYR88
B	ALA116
B	GLY118
B	VAL195
B	PHE200
B	GLU201
B	VAL217
B	GLY218
B	MET219
B	THR242
B	ASN243
B	HIS257
B	VAL260
B	PO4301
B	HOH416
B	HOH452
C	TYR159

---

site_id	AD6
Number of Residues	11
Details	binding site for residue PO4 C 301

Chain	Residue
C	HIS86
C	ASN115
C	ALA116
C	SER220
C	IM5305
C	HOH407
C	HOH411
C	GLY32
C	SER33
C	HIS64
C	ARG84

---

site_id	AD7
Number of Residues	4
Details	binding site for residue PO4 C 302

Chain	Residue
B	PRO92
B	GLN144
C	ARG148
C	HOH444

---

site_id	AD8
Number of Residues	4
Details	binding site for residue PO4 C 303

Chain	Residue
B	TYR249
C	ARG133
C	ARG168
C	ARG171

---

site_id	AD9
Number of Residues	4
Details	binding site for residue PO4 C 304

Chain	Residue
C	THR6
C	TYR7
C	GLU8
C	ARG154

---

site_id	AE1
Number of Residues	15
Details	binding site for residue IM5 C 305

Chain	Residue
A	TYR159
C	TYR88
C	ALA116
C	GLY118
C	VAL195
C	PHE200
C	GLU201
C	VAL217
C	GLY218
C	MET219
C	THR242
C	ASN243
C	HIS257
C	PO4301
C	HOH438

---

site_id	AE2
Number of Residues	10
Details	binding site for residue PO4 D 301

Chain	Residue
D	GLY32
D	SER33
D	HIS64
D	ARG84
D	HIS86
D	ASN115
D	ALA116
D	SER220
D	IM5307
D	HOH410

---

site_id	AE3
Number of Residues	4
Details	binding site for residue PO4 D 302

Chain	Residue
D	ARG148
F	PRO92
F	GLN144
F	HOH413

---

site_id	AE4
Number of Residues	4
Details	binding site for residue PO4 D 303

Chain	Residue
D	PRO92
D	GLN144
D	HOH420
E	ARG148

---

site_id	AE5
Number of Residues	4
Details	binding site for residue PO4 D 304

Chain	Residue
D	ARG133
D	HOH402
F	ARG207
F	TYR249

---

site_id	AE6
Number of Residues	4
Details	binding site for residue PO4 D 305

Chain	Residue
D	ARG207
D	TYR249
D	HOH424
E	ARG133

---

site_id	AE7
Number of Residues	3
Details	binding site for residue PO4 D 306

Chain	Residue
D	ARG133
D	ARG168
D	ARG171

---

site_id	AE8
Number of Residues	17
Details	binding site for residue IM5 D 307

Chain	Residue
D	TYR88
D	ALA116
D	ALA117
D	GLY118
D	VAL195
D	PHE200
D	GLU201
D	VAL217
D	GLY218
D	MET219
D	THR242
D	ASN243
D	HIS257
D	VAL260
D	PO4301
D	HOH432
E	TYR159

---

site_id	AE9
Number of Residues	11
Details	binding site for residue PO4 E 301

Chain	Residue
E	GLY32
E	SER33
E	HIS64
E	ARG84
E	HIS86
E	ASN115
E	ALA116
E	SER220
E	IM5306
E	HOH401
E	HOH433

---

site_id	AF1
Number of Residues	4
Details	binding site for residue PO4 E 302

Chain	Residue
E	PRO92
E	GLN144
E	HOH402
F	ARG148

---

site_id	AF2
Number of Residues	1
Details	binding site for residue PO4 E 303

Chain	Residue
E	GLN44

---

site_id	AF3
Number of Residues	4
Details	binding site for residue PO4 E 304

Chain	Residue
E	ARG133
E	ARG168
E	ARG171
E	HOH419

---

site_id	AF4
Number of Residues	3
Details	binding site for residue PO4 E 305

Chain	Residue
E	ARG207
E	HOH415
F	ARG133

---

site_id	AF5
Number of Residues	15
Details	binding site for residue IM5 E 306

Chain	Residue
E	TYR88
E	ALA116
E	GLY118
E	PHE200
E	GLU201
E	VAL217
E	GLY218
E	MET219
E	THR242
E	ASN243
E	HIS257
E	VAL260
E	PO4301
E	HOH427
F	TYR159

---

site_id	AF6
Number of Residues	11
Details	binding site for residue PO4 F 301

Chain	Residue
F	GLY32
F	SER33
F	HIS64
F	ARG84
F	HIS86
F	ASN115
F	ALA116
F	SER220
F	IM5303
F	HOH411
F	HOH415

---

site_id	AF7
Number of Residues	4
Details	binding site for residue PO4 F 302

Chain	Residue
E	TYR249
F	ARG133
F	ARG168
F	ARG171

---

site_id	AF8
Number of Residues	17
Details	binding site for residue IM5 F 303

Chain	Residue
D	TYR159
F	TYR88
F	ALA116
F	ALA117
F	GLY118
F	PHE200
F	GLU201
F	VAL217
F	GLY218
F	MET219
F	THR242
F	ASN243
F	HIS257
F	VAL260
F	PO4301
F	HOH415
F	HOH440

---

Functional Information from PROSITE/UniProt

site_id	PS01240
Number of Residues	42
Details	PNP_MTAP_2 Purine and other phosphorylases family 2 signature. VmmqGrfHmYegypLwkvTfpVrVfhllGvdt.LVvtNAaGGL

Chain	Residue	Details
A	VAL79-LEU120

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23438750","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14706628","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"1763067","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1RCT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ULA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ULB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EAR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EB8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GKA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P55859","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23438750","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14706628","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"1763067","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1RCT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ULA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ULB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1V3Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EAR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EB8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GKA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14706628","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23438750","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RCT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EAR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EB8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14706628","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23438750","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1763067","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1RCT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ULB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EAR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EB8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GKA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14706628","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RCT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	Site: {"description":"Important for substrate specificity","evidences":[{"source":"PubMed","id":"9305964","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2006","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Claeys D."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	10
Details	M-CSA 17

Chain	Residue	Details
A	SER33	hydrogen bond donor
A	HIS257	electrostatic stabiliser, hydrogen bond acceptor
A	HIS64	electrostatic stabiliser
A	HIS86	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	TYR88	electrostatic stabiliser, hydrogen bond donor
A	GLU89	activator, electrostatic stabiliser, hydrogen bond acceptor
A	ALA116	electrostatic stabiliser, hydrogen bond donor
A	MET219	electrostatic stabiliser, hydrogen bond donor
A	SER220	electrostatic stabiliser, hydrogen bond donor
A	ASN243	electrostatic stabiliser, hydrogen bond donor, polar interaction

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site_id	MCSA2
Number of Residues	10
Details	M-CSA 17

Chain	Residue	Details
B	SER33	hydrogen bond donor
B	HIS257	electrostatic stabiliser, hydrogen bond acceptor
B	HIS64	electrostatic stabiliser
B	HIS86	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	TYR88	electrostatic stabiliser, hydrogen bond donor
B	GLU89	activator, electrostatic stabiliser, hydrogen bond acceptor
B	ALA116	electrostatic stabiliser, hydrogen bond donor
B	MET219	electrostatic stabiliser, hydrogen bond donor
B	SER220	electrostatic stabiliser, hydrogen bond donor
B	ASN243	electrostatic stabiliser, hydrogen bond donor, polar interaction

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site_id	MCSA3
Number of Residues	10
Details	M-CSA 17

Chain	Residue	Details
C	SER33	hydrogen bond donor
C	HIS257	electrostatic stabiliser, hydrogen bond acceptor
C	HIS64	electrostatic stabiliser
C	HIS86	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	TYR88	electrostatic stabiliser, hydrogen bond donor
C	GLU89	activator, electrostatic stabiliser, hydrogen bond acceptor
C	ALA116	electrostatic stabiliser, hydrogen bond donor
C	MET219	electrostatic stabiliser, hydrogen bond donor
C	SER220	electrostatic stabiliser, hydrogen bond donor
C	ASN243	electrostatic stabiliser, hydrogen bond donor, polar interaction

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site_id	MCSA4
Number of Residues	10
Details	M-CSA 17

Chain	Residue	Details
D	SER33	hydrogen bond donor
D	HIS257	electrostatic stabiliser, hydrogen bond acceptor
D	HIS64	electrostatic stabiliser
D	HIS86	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	TYR88	electrostatic stabiliser, hydrogen bond donor
D	GLU89	activator, electrostatic stabiliser, hydrogen bond acceptor
D	ALA116	electrostatic stabiliser, hydrogen bond donor
D	MET219	electrostatic stabiliser, hydrogen bond donor
D	SER220	electrostatic stabiliser, hydrogen bond donor
D	ASN243	electrostatic stabiliser, hydrogen bond donor, polar interaction

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site_id	MCSA5
Number of Residues	10
Details	M-CSA 17

Chain	Residue	Details
E	SER33	hydrogen bond donor
E	HIS257	electrostatic stabiliser, hydrogen bond acceptor
E	HIS64	electrostatic stabiliser
E	HIS86	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	TYR88	electrostatic stabiliser, hydrogen bond donor
E	GLU89	activator, electrostatic stabiliser, hydrogen bond acceptor
E	ALA116	electrostatic stabiliser, hydrogen bond donor
E	MET219	electrostatic stabiliser, hydrogen bond donor
E	SER220	electrostatic stabiliser, hydrogen bond donor
E	ASN243	electrostatic stabiliser, hydrogen bond donor, polar interaction

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site_id	MCSA6
Number of Residues	10
Details	M-CSA 17

Chain	Residue	Details
F	SER33	hydrogen bond donor
F	HIS257	electrostatic stabiliser, hydrogen bond acceptor
F	HIS64	electrostatic stabiliser
F	HIS86	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	TYR88	electrostatic stabiliser, hydrogen bond donor
F	GLU89	activator, electrostatic stabiliser, hydrogen bond acceptor
F	ALA116	electrostatic stabiliser, hydrogen bond donor
F	MET219	electrostatic stabiliser, hydrogen bond donor
F	SER220	electrostatic stabiliser, hydrogen bond donor
F	ASN243	electrostatic stabiliser, hydrogen bond donor, polar interaction

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