3QVI

Crystal structure of KNI-10395 bound histo-aspartic protease (HAP) from Plasmodium falciparum

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004190	molecular_function	aspartic-type endopeptidase activity
A	0005775	cellular_component	vacuolar lumen
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0020020	cellular_component	food vacuole
A	0044002	biological_process	acquisition of nutrients from host
B	0004190	molecular_function	aspartic-type endopeptidase activity
B	0005775	cellular_component	vacuolar lumen
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0016020	cellular_component	membrane
B	0016787	molecular_function	hydrolase activity
B	0020020	cellular_component	food vacuole
B	0044002	biological_process	acquisition of nutrients from host
C	0004190	molecular_function	aspartic-type endopeptidase activity
C	0005775	cellular_component	vacuolar lumen
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0016020	cellular_component	membrane
C	0016787	molecular_function	hydrolase activity
C	0020020	cellular_component	food vacuole
C	0044002	biological_process	acquisition of nutrients from host
D	0004190	molecular_function	aspartic-type endopeptidase activity
D	0005775	cellular_component	vacuolar lumen
D	0006508	biological_process	proteolysis
D	0008233	molecular_function	peptidase activity
D	0016020	cellular_component	membrane
D	0016787	molecular_function	hydrolase activity
D	0020020	cellular_component	food vacuole
D	0044002	biological_process	acquisition of nutrients from host

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE K95 A 329

Chain	Residue
A	HIS32
A	ALA34
A	SER35
A	LEU128
A	LEU291
A	HOH350
A	HOH607
B	GLU278
B	HOH364

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE K95 C 329

Chain	Residue
C	HIS32
C	ALA34
C	SER35
C	LEU128
C	ASP215
C	GLU292
C	HOH365
D	GLU278
D	ALA280
D	HOH666
D	HOH710

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE K95 C 330

Chain	Residue
C	GLU278
C	LEU281
C	HOH338
C	HOH556
C	HOH592
D	HIS32
D	ALA34
D	SER35
D	MET189
D	ASP215
D	EDO332

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA D 329

Chain	Residue
B	ARG261
D	ARG261

---

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO C 331

Chain	Residue
C	SER36
C	GLY122
C	LEU123
C	GLY124
C	PRO135
C	TYR136
C	HOH398
C	HOH828

---

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 329

Chain	Residue
A	PHE111
A	HOH383
B	PRO277
B	GLU278
B	ASN279
B	ILE279
B	SER279
B	HOH581

---

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO D 330

Chain	Residue
C	PHE111
D	PRO277
D	GLU278
D	ASN279
D	ILE279
D	SER279
D	HOH557
D	HOH600
D	HOH762

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 330

Chain	Residue
A	LYS66
A	LYS100
A	GLN230

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 332

Chain	Residue
C	GLN143
C	LYS145
D	LYS19

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 333

Chain	Residue
C	PRO98
C	LYS145
D	ASP22
D	HOH362

---

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 331

Chain	Residue
D	LYS100
D	GLU226
D	ASN229
D	GLU233

---

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO D 332

Chain	Residue
C	K95330
D	SER35
D	SER36
D	ASN37
D	TRP39
D	LEU128

---

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO D 333

Chain	Residue
C	THR63
C	GLU65
C	LYS86
C	PRO98
D	ASN23
D	HOH817

---

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 331

Chain	Residue
A	SER219
A	GLU276
A	ASN285
B	GLU276
B	PG5330

---

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 334

Chain	Residue
C	ASP67
C	THR69
C	LYS100
C	GLY131

---

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PG5 B 330

Chain	Residue
B	MET283
A	GLU276
A	MET283
A	ASN285
A	EDO331
B	VAL220
B	GLU276

---

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PG4 D 334

Chain	Residue
B	ARG261
D	ASP193
D	ASP195
D	LYS209
D	ARG261
D	SER262
D	PRO263

---

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PG4 A 333

Chain	Residue
A	PRO70
A	VAL71
A	LYS72
A	SER236

---

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PG4 A 334

Chain	Residue
A	SER95
A	PRO98
A	LYS145

---

site_id	CC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PG4 A 335

Chain	Residue
A	LYS183
B	ASN203
B	PHE238

---

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT A 336

Chain	Residue
A	ASN144
A	LYS145
A	ILE146
A	GLU147

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	921
Details	Domain: {"description":"Peptidase A1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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