5Y1X

Crystal structure of Plasmodium falciparum aminopeptidase N in complex with actinonin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 1101

Chain	Residue
A	HIS496
A	HIS500
A	GLU519
A	BB21103

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site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 1102

Chain	Residue
A	HOH1776
A	HOH1507
A	HOH1550
A	HOH1560
A	HOH1740
A	HOH1762

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site_id	AC3
Number of Residues	18
Details	binding site for residue BB2 A 1103

Chain	Residue
A	ASN458
A	VAL459
A	GLY460
A	ALA461
A	GLU463
A	ARG489
A	HIS496
A	GLU497
A	HIS500
A	GLU519
A	TYR580
A	GLN1038
A	ZN1101
A	HOH1203
A	HOH1262
A	HOH1370
A	HOH1656
A	HOH1675

---

site_id	AC4
Number of Residues	5
Details	binding site for residue GOL A 1104

Chain	Residue
A	TYR853
A	SER903
A	LEU904
A	LYS907
A	TYR938

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Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVGHEYFHNY

Chain	Residue	Details
A	VAL493-TYR502

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P15144

Chain	Residue	Details
A	GLU497

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:19196988, ECO:0000305|PubMed:21366301, ECO:0007744|PDB:3EBH, ECO:0007744|PDB:3EBI, ECO:0007744|PDB:3Q43

Chain	Residue	Details
A	GLU319
A	GLY460
A	GLU463

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305|PubMed:19196988, ECO:0000305|PubMed:21366301, ECO:0007744|PDB:3EBH, ECO:0007744|PDB:3Q43

Chain	Residue	Details
A	ALA461

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:19196988, ECO:0000269|PubMed:21366301, ECO:0000269|PubMed:21844374, ECO:0000269|PubMed:23713488, ECO:0000269|PubMed:23897806, ECO:0000269|PubMed:25299353, ECO:0000269|PubMed:25645579, ECO:0000269|PubMed:26406322, ECO:0000269|PubMed:26807544, ECO:0000269|PubMed:30537832, ECO:0000269|PubMed:32182520, ECO:0000269|Ref.21, ECO:0000269|DOI:10.1016/j.cclet.2021.09.102, ECO:0000312|PDB:3T8V, ECO:0000312|PDB:5Y1Q, ECO:0007744|PDB:3EBG, ECO:0007744|PDB:3EBH, ECO:0007744|PDB:3EBI, ECO:0007744|PDB:3Q43, ECO:0007744|PDB:3Q44, ECO:0007744|PDB:4J3B, ECO:0007744|PDB:4K5L, ECO:0007744|PDB:4K5M, ECO:0007744|PDB:4K5N, ECO:0007744|PDB:4K5O, ECO:0007744|PDB:4K5P, ECO:0007744|PDB:4R5T, ECO:0007744|PDB:4R5V, ECO:0007744|PDB:4R5X, ECO:0007744|PDB:4X2U, ECO:0007744|PDB:4ZQT, ECO:0007744|PDB:4ZW3, ECO:0007744|PDB:4ZW5, ECO:0007744|PDB:4ZW6, ECO:0007744|PDB:4ZW7, ECO:0007744|PDB:4ZW8, ECO:0007744|PDB:4ZX3, ECO:0007744|PDB:4ZX4, ECO:0007744|PDB:4ZX5, ECO:0007744|PDB:4ZX6, ECO:0007744|PDB:5XM7, ECO:0007744|PDB:5Y19, ECO:0007744|PDB:5Y1H, ECO:0007744|PDB:5Y1K, ECO:0007744|PDB:5Y1R, ECO:0007744|PDB:5Y1S, ECO:0007744|PDB:5Y1T, ECO:0007744|PDB:5Y1V, ECO:0007744|PDB:5Y1W, ECO:0007744|PDB:5Y1X, ECO:0007744|PDB:5Y3I, ECO:0007744|PDB:6EA1, ECO:0007744|PDB:6EA2, ECO:0007744|PDB:6EAA, ECO:0007744|PDB:6EAB, ECO:0007744|PDB:6EE3, ECO:0007744|PDB:6EE4, ECO:0007744|PDB:6EE6, ECO:0007744|PDB:6EED, ECO:0007744|PDB:6SBQ, ECO:0007744|PDB:6SBR

Chain	Residue	Details
A	HIS496
A	HIS500
A	GLU519

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Important for substrate specificity => ECO:0000269|PubMed:23897806

Chain	Residue	Details
A	VAL459

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site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P15144

Chain	Residue	Details
A	TYR580

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	SITE: Cleavage => ECO:0000305|PubMed:21659511

Chain	Residue	Details
A	ASN795

---