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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3EBH

Structure of the M1 Alanylaminopeptidase from malaria complexed with bestatin

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	BES1085

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BES A1085

Chain	Residue
A	ALA461
A	GLU463
A	HIS496
A	GLU497
A	HIS500
A	LYS518
A	GLU519
A	TYR575
A	TYR580
A	HOH1604
A	ZN1
A	GOL6
A	GLU319
A	VAL459
A	GLY460

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A1086

Chain	Residue
A	HOH19
A	LYS479
A	TYR880
A	HIS886
A	VAL887
A	ASP888
A	GLN891
A	ARG895
A	TYR925
A	HOH1500

site_id	AC4
Number of Residues	9
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	HOH1489
A	HOH1668

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 3

Chain	Residue
A	HOH105
A	HIS653
A	LYS676
A	TYR741
A	ASN835
A	PHE836
A	HOH1661

site_id	AC6
Number of Residues	10
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	ASN994
A	ARG997
A	HOH1604

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 5

Chain	Residue
A	ILE483
A	THR931
A	SER934
A	THR966
A	HOH1116
A	HOH1153
A	HOH1363
A	HOH1584

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 6

Chain	Residue
A	TYR575
A	TYR580
A	BES1085
A	HOH1198
A	HOH1648

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 7

Chain	Residue
A	HOH26
A	GLY250
A	HOH1099
A	HOH1212
A	HOH1520
A	HOH1521

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 8

Chain	Residue
A	HOH1176
A	HOH1523
A	HOH1524
A	HOH1525
A	HOH1526
A	HOH1527

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 9

Chain	Residue
A	GLU957
A	HOH1541
A	HOH1542
A	HOH1543
A	HOH1544

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 10

Chain	Residue
A	HOH100
A	HOH103
A	HOH1461
A	HOH1566
A	HOH1567

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	GLU463
A	GLU319
A	GLY460

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

219869

PDB entries from 2024-05-15

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