Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3EBI

Structure of the M1 Alanylaminopeptidase from malaria complexed with the phosphinate dipeptide analog

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 1

Chain	Residue
A	HIS496
A	HIS500
A	GLU519
A	BEY1085

site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE BEY A1085

Chain	Residue
A	ALA461
A	MET462
A	GLU463
A	ARG489
A	VAL493
A	HIS496
A	GLU497
A	HIS500
A	GLU519
A	TYR575
A	TYR580
A	MET1034
A	HOH1544
A	HOH1545
A	ZN1
A	GLN317
A	GLU319
A	VAL459
A	GLY460

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL A1086

Chain	Residue
A	HOH19
A	LYS479
A	TYR880
A	HIS886
A	VAL887
A	ASP888
A	GLN891
A	MET892
A	ARG895
A	TYR925
A	HOH1513

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 10

Chain	Residue
A	HOH100
A	HOH103
A	HOH1473
A	HOH1542
A	HOH1543

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 2

Chain	Residue
A	TYR765
A	CYS768
A	THR769
A	TYR772
A	TYR823
A	SER826
A	PRO828
A	HOH1502

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 3

Chain	Residue
A	HOH105
A	HIS653
A	LYS676
A	TYR741
A	ASN835
A	HOH1417

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 4

Chain	Residue
A	HOH62
A	VAL459
A	GLY460
A	ASN471
A	ASN473
A	SER474
A	ARG489
A	ARG997

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 5

Chain	Residue
A	ILE483
A	LEU930
A	THR931
A	SER934
A	THR966
A	ARG969
A	HOH1116
A	HOH1154
A	HOH1369

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 7

Chain	Residue
A	HOH26
A	GLY250
A	HOH1099
A	HOH1214
A	HOH1536

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 8

Chain	Residue
A	HOH1177
A	HOH1537
A	HOH1538
A	HOH1539
A	HOH1540

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 9

Chain	Residue
A	GLU957
A	HOH1541

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL493-TYR502

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

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	GLN795

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1h19

Chain	Residue	Details
A	TYR580
A	GLU463
A	GLU497

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