Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6EE6

X-ray crystal structure of Pf-M1 in complex with inhibitor (6o) and catalytic zinc ion

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	J4P1102

site_id	AC2
Number of Residues	21
Details	binding site for residue J4P A 1102

Chain	Residue
A	VAL459
A	GLY460
A	ALA461
A	GLU463
A	ARG489
A	THR492
A	HIS496
A	GLU497
A	HIS500
A	GLU519
A	GLU572
A	TYR575
A	TYR580
A	MET1034
A	ZN1101
A	GOL1105
A	THR305
A	GLN317
A	GLU319
A	ALA320
A	ASN458

site_id	AC3
Number of Residues	7
Details	binding site for residue GOL A 1103

Chain	Residue
A	VAL245
A	ASP247
A	PHE275
A	ILE330
A	HOH1211
A	HOH1332
A	HOH1497

site_id	AC4
Number of Residues	7
Details	binding site for residue GOL A 1104

Chain	Residue
A	ASN573
A	TYR575
A	THR576
A	THR1037
A	GLN1038
A	TYR1077
A	HOH1306

site_id	AC5
Number of Residues	8
Details	binding site for residue GOL A 1105

Chain	Residue
A	TYR575
A	THR576
A	THR577
A	J4P1102
A	HOH1320
A	HOH1711
A	HOH1800
A	HOH1958

site_id	AC6
Number of Residues	11
Details	binding site for residue GOL A 1106

Chain	Residue
A	VAL459
A	ASN471
A	ASN473
A	SER474
A	ARG489
A	ASN994
A	ARG997
A	HOH1236
A	HOH1319
A	HOH1891
A	HOH2051

site_id	AC7
Number of Residues	3
Details	binding site for residue GOL A 1107

Chain	Residue
A	HIS886
A	VAL887
A	ASP888

site_id	AC8
Number of Residues	6
Details	binding site for residue MG A 1108

Chain	Residue
A	GLY250
A	HOH1608
A	HOH1831
A	HOH1956
A	HOH2034
A	HOH2037

site_id	AC9
Number of Residues	7
Details	binding site for residue MG A 1109

Chain	Residue
A	GLU957
A	HOH1444
A	HOH1553
A	HOH1738
A	HOH2311
A	HOH2455
A	HOH2504

site_id	AD1
Number of Residues	6
Details	binding site for residue MG A 1110

Chain	Residue
A	HOH1422
A	HOH1723
A	HOH1930
A	HOH2249
A	HOH2460
A	HOH2567

site_id	AD2
Number of Residues	9
Details	binding site for residue GOL A 1111

Chain	Residue
A	THR305
A	ARG325
A	GLU572
A	PRO1033
A	HOH1351
A	HOH1465
A	HOH1922
A	HOH1985
A	HOH2026

site_id	AD3
Number of Residues	10
Details	binding site for residue GOL A 1112

Chain	Residue
A	LYS479
A	HIS886
A	VAL887
A	ASP888
A	GLN891
A	MET892
A	ARG895
A	TYR925
A	HOH1209
A	HOH1372

site_id	AD4
Number of Residues	9
Details	binding site for residue GOL A 1113

Chain	Residue
A	ASP545
A	TYR765
A	CYS768
A	THR769
A	TYR772
A	TYR823
A	SER826
A	PRO828
A	HOH1605

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

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