Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7RIE

Plasmodium falciparum M17 in complex with inhibitor MIPS2571

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0006508	biological_process	proteolysis
A	0019538	biological_process	protein metabolic process
A	0030145	molecular_function	manganese ion binding
A	0046872	molecular_function	metal ion binding
A	0070006	molecular_function	metalloaminopeptidase activity
B	0005737	cellular_component	cytoplasm
B	0006508	biological_process	proteolysis
B	0019538	biological_process	protein metabolic process
B	0030145	molecular_function	manganese ion binding
B	0046872	molecular_function	metal ion binding
B	0070006	molecular_function	metalloaminopeptidase activity
C	0005737	cellular_component	cytoplasm
C	0006508	biological_process	proteolysis
C	0019538	biological_process	protein metabolic process
C	0030145	molecular_function	manganese ion binding
C	0046872	molecular_function	metal ion binding
C	0070006	molecular_function	metalloaminopeptidase activity
D	0005737	cellular_component	cytoplasm
D	0006508	biological_process	proteolysis
D	0019538	biological_process	protein metabolic process
D	0030145	molecular_function	manganese ion binding
D	0046872	molecular_function	metal ion binding
D	0070006	molecular_function	metalloaminopeptidase activity
E	0005737	cellular_component	cytoplasm
E	0006508	biological_process	proteolysis
E	0019538	biological_process	protein metabolic process
E	0030145	molecular_function	manganese ion binding
E	0046872	molecular_function	metal ion binding
E	0070006	molecular_function	metalloaminopeptidase activity
F	0005737	cellular_component	cytoplasm
F	0006508	biological_process	proteolysis
F	0019538	biological_process	protein metabolic process
F	0030145	molecular_function	manganese ion binding
F	0046872	molecular_function	metal ion binding
F	0070006	molecular_function	metalloaminopeptidase activity
G	0005737	cellular_component	cytoplasm
G	0006508	biological_process	proteolysis
G	0019538	biological_process	protein metabolic process
G	0030145	molecular_function	manganese ion binding
G	0046872	molecular_function	metal ion binding
G	0070006	molecular_function	metalloaminopeptidase activity
H	0005737	cellular_component	cytoplasm
H	0006508	biological_process	proteolysis
H	0019538	biological_process	protein metabolic process
H	0030145	molecular_function	manganese ion binding
H	0046872	molecular_function	metal ion binding
H	0070006	molecular_function	metalloaminopeptidase activity
I	0005737	cellular_component	cytoplasm
I	0006508	biological_process	proteolysis
I	0019538	biological_process	protein metabolic process
I	0030145	molecular_function	manganese ion binding
I	0046872	molecular_function	metal ion binding
I	0070006	molecular_function	metalloaminopeptidase activity
J	0005737	cellular_component	cytoplasm
J	0006508	biological_process	proteolysis
J	0019538	biological_process	protein metabolic process
J	0030145	molecular_function	manganese ion binding
J	0046872	molecular_function	metal ion binding
J	0070006	molecular_function	metalloaminopeptidase activity
K	0005737	cellular_component	cytoplasm
K	0006508	biological_process	proteolysis
K	0019538	biological_process	protein metabolic process
K	0030145	molecular_function	manganese ion binding
K	0046872	molecular_function	metal ion binding
K	0070006	molecular_function	metalloaminopeptidase activity
L	0005737	cellular_component	cytoplasm
L	0006508	biological_process	proteolysis
L	0019538	biological_process	protein metabolic process
L	0030145	molecular_function	manganese ion binding
L	0046872	molecular_function	metal ion binding
L	0070006	molecular_function	metalloaminopeptidase activity

Functional Information from PROSITE/UniProt

site_id	PS00631
Number of Residues	8
Details	CYTOSOL_AP Cytosol aminopeptidase signature. NTDAEGRL

Chain	Residue	Details
A	ASN457-LEU464

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	ACT_SITE: ACT_SITE => ECO:0000250\|UniProtKB:P00727

Chain	Residue	Details
A	LYS386
A	ARG463
B	LYS386
B	ARG463
C	LYS386
C	ARG463
D	LYS386
D	ARG463
E	LYS386
E	ARG463
F	LYS386
F	ARG463
G	LYS386
G	ARG463
H	LYS386
H	ARG463
I	LYS386
I	ARG463
J	LYS386
J	ARG463
K	LYS386
K	ARG463
L	LYS386
L	ARG463

site_id	SWS_FT_FI2
Number of Residues	36
Details	BINDING: BINDING => ECO:0000269\|PubMed:20133789, ECO:0000269\|PubMed:21844374, ECO:0000269\|PubMed:23713488, ECO:0000269\|PubMed:25299353, ECO:0000269\|PubMed:25645579, ECO:0000269\|PubMed:35691342, ECO:0000269\|Ref.13, ECO:0000312\|PDB:3T8W, ECO:0007744\|PDB:3KQX, ECO:0007744\|PDB:3KQZ, ECO:0007744\|PDB:3KR4, ECO:0007744\|PDB:3KR5, ECO:0007744\|PDB:4K3N, ECO:0007744\|PDB:4R6T, ECO:0007744\|PDB:4R76, ECO:0007744\|PDB:4R7M, ECO:0007744\|PDB:4X2T, ECO:0007744\|PDB:7RIE, ECO:0007744\|PDB:7T3V

Chain	Residue	Details
A	LYS374
A	ASP379
A	GLU461
B	LYS374
B	ASP379
B	GLU461
C	LYS374
C	ASP379
C	GLU461
D	LYS374
D	ASP379
D	GLU461
E	LYS374
E	ASP379
E	GLU461
F	LYS374
F	ASP379
F	GLU461
G	LYS374
G	ASP379
G	GLU461
H	LYS374
H	ASP379
H	GLU461
I	LYS374
I	ASP379
I	GLU461
J	LYS374
J	ASP379
J	GLU461
K	LYS374
K	ASP379
K	GLU461
L	LYS374
L	ASP379
L	GLU461

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000305\|PubMed:20133789, ECO:0000305\|PubMed:23713488, ECO:0007744\|PDB:3KR5, ECO:0007744\|PDB:4K3N

Chain	Residue	Details
A	LYS386
B	LYS386
C	LYS386
D	LYS386
E	LYS386
F	LYS386
G	LYS386
H	LYS386
I	LYS386
J	LYS386
K	LYS386
L	LYS386

site_id	SWS_FT_FI4
Number of Residues	36
Details	BINDING: BINDING => ECO:0000269\|PubMed:35691342, ECO:0007744\|PDB:7SRV

Chain	Residue	Details
A	ASP394
A	MET396
A	ASP399
B	ASP394
B	MET396
B	ASP399
C	ASP394
C	MET396
C	ASP399
D	ASP394
D	MET396
D	ASP399
E	ASP394
E	MET396
E	ASP399
F	ASP394
F	MET396
F	ASP399
G	ASP394
G	MET396
G	ASP399
H	ASP394
H	MET396
H	ASP399
I	ASP394
I	MET396
I	ASP399
J	ASP394
J	MET396
J	ASP399
K	ASP394
K	MET396
K	ASP399
L	ASP394
L	MET396
L	ASP399

site_id	SWS_FT_FI5
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:20133789, ECO:0000269\|PubMed:21844374, ECO:0000269\|PubMed:23713488, ECO:0000269\|PubMed:25299353, ECO:0000269\|PubMed:25645579, ECO:0000269\|PubMed:35691342, ECO:0000269\|Ref.13, ECO:0000312\|PDB:3KQZ, ECO:0000312\|PDB:3T8W, ECO:0007744\|PDB:3KR4, ECO:0007744\|PDB:3KR5, ECO:0007744\|PDB:4K3N, ECO:0007744\|PDB:4R6T, ECO:0007744\|PDB:4R76, ECO:0007744\|PDB:4R7M, ECO:0007744\|PDB:4X2T, ECO:0007744\|PDB:7RIE, ECO:0007744\|PDB:7T3V

Chain	Residue	Details
A	ASP459
B	ASP459
C	ASP459
D	ASP459
E	ASP459
F	ASP459
G	ASP459
H	ASP459
I	ASP459
J	ASP459
K	ASP459
L	ASP459

site_id	SWS_FT_FI6
Number of Residues	12
Details	SITE: Essential for hexamer stabilization => ECO:0000269\|PubMed:35691342

Chain	Residue	Details
A	LYS386
B	LYS386
C	LYS386
D	LYS386
E	LYS386
F	LYS386
G	LYS386
H	LYS386
I	LYS386
J	LYS386
K	LYS386
L	LYS386

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)