Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3B7U

Leukotriene A4 Hydrolase Complexed with KELatorphan

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0003723	molecular_function	RNA binding
X	0004177	molecular_function	aminopeptidase activity
X	0004301	molecular_function	epoxide hydrolase activity
X	0004463	molecular_function	leukotriene-A4 hydrolase activity
X	0005515	molecular_function	protein binding
X	0005576	cellular_component	extracellular region
X	0005634	cellular_component	nucleus
X	0005654	cellular_component	nucleoplasm
X	0005737	cellular_component	cytoplasm
X	0005829	cellular_component	cytosol
X	0006508	biological_process	proteolysis
X	0006629	biological_process	lipid metabolic process
X	0006691	biological_process	leukotriene metabolic process
X	0008233	molecular_function	peptidase activity
X	0008237	molecular_function	metallopeptidase activity
X	0008270	molecular_function	zinc ion binding
X	0010043	biological_process	response to zinc ion
X	0019370	biological_process	leukotriene biosynthetic process
X	0019538	biological_process	protein metabolic process
X	0043171	biological_process	peptide catabolic process
X	0043434	biological_process	response to peptide hormone
X	0045148	molecular_function	tripeptide aminopeptidase activity
X	0046872	molecular_function	metal ion binding
X	0060509	biological_process	type I pneumocyte differentiation
X	0070006	molecular_function	metalloaminopeptidase activity
X	0070062	cellular_component	extracellular exosome
X	1904724	cellular_component	tertiary granule lumen
X	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN X 701

Chain	Residue
X	HIS295
X	HIS299
X	GLU318

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE YB X 702

Chain	Residue
X	ASP47
X	ASP481
X	HOH747
X	HOH771

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE YB X 703

Chain	Residue
X	HOH1085
X	ASP426
X	ASP610

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE YB X 704

Chain	Residue
X	ASP175
X	HOH1081

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE IMD X 705

Chain	Residue
X	GLY344
X	GLY347
X	GLU348
X	ASN351
X	GLU501
X	ALA504
X	GLN508

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE KEL X 707

Chain	Residue
X	TYR267
X	GLY268
X	GLY269
X	GLU271
X	ASN291
X	HIS295
X	GLU296
X	HIS299
X	GLU318
X	TYR378
X	TYR383
X	ARG563
X	LYS565
X	HOH734
X	HOH822
X	HOH958
X	HOH969

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACY X 706

Chain	Residue
X	ASP47
X	ASN48
X	ARG174
X	LYS479
X	ASP481
X	HOH741
X	HOH771

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
X	VAL292-TRP301

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:11675384, ECO:0000305\|PubMed:12207002, ECO:0000305\|PubMed:24591641, ECO:0007744\|PDB:1H19

Chain	Residue	Details
X	GLU296

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269\|PubMed:11675384, ECO:0000305\|PubMed:12207002, ECO:0000305\|PubMed:24591641, ECO:0007744\|PDB:1H19

Chain	Residue	Details
X	TYR383

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:18804029

Chain	Residue	Details
X	GLN134
X	PRO266
X	ARG563

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11175901, ECO:0000269\|PubMed:11675384, ECO:0000269\|PubMed:11917124, ECO:0000269\|PubMed:12207002, ECO:0000269\|PubMed:15078870, ECO:0000269\|PubMed:18804029, ECO:0000269\|PubMed:19618939, ECO:0000269\|PubMed:24591641, ECO:0007744\|PDB:1GW6, ECO:0007744\|PDB:1H19, ECO:0007744\|PDB:1HS6, ECO:0007744\|PDB:1SQM, ECO:0007744\|PDB:2R59, ECO:0007744\|PDB:2VJ8, ECO:0007744\|PDB:3B7R, ECO:0007744\|PDB:3B7S, ECO:0007744\|PDB:3B7T, ECO:0007744\|PDB:3B7U, ECO:0007744\|PDB:3CHO, ECO:0007744\|PDB:3CHP, ECO:0007744\|PDB:3CHQ, ECO:0007744\|PDB:3CHR, ECO:0007744\|PDB:3CHS, ECO:0007744\|PDB:3FH5, ECO:0007744\|PDB:3FH7, ECO:0007744\|PDB:3FH8, ECO:0007744\|PDB:3FHE, ECO:0007744\|PDB:3FTS, ECO:0007744\|PDB:3FTU, ECO:0007744\|PDB:3FTV, ECO:0007744\|PDB:3FTW, ECO:0007744\|PDB:3FTX, ECO:0007744\|PDB:3FTY, ECO:0007744\|PDB:3FTZ, ECO:0007744\|PDB:3FU0, ECO:0007744\|PDB:3FU3, ECO:0007744\|PDB:3FU5, ECO:0007744\|PDB:3FU6, ECO:0007744\|PDB:3FUD, ECO:0007744\|PDB:3FUE, ECO:0007744\|PDB:3FUF, ECO:0007744\|PDB:3FUH, ECO:0007744\|PDB:3FUI, ECO:0007744\|PDB:3FUJ, ECO:0007744\|PDB:3FUK, ECO:0007744\|PDB:3FUL, ECO:0007744\|PDB:3FUM, ECO:0007744\|PDB:3FUN, ECO:0007744\|PDB:3U9W, ECO:0007744\|PDB:4DPR, ECO:0007744\|PDB:4L2L, ECO:0007744\|PDB:4MKT, ECO:0007744\|PDB:4MS6, ECO:0007744\|PDB:5AEN

Chain	Residue	Details
X	HIS295
X	HIS299

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:11175901, ECO:0000269\|PubMed:24591641, ECO:0007744\|PDB:1GW6, ECO:0007744\|PDB:1H19, ECO:0007744\|PDB:1HS6, ECO:0007744\|PDB:1SQM, ECO:0007744\|PDB:2R59, ECO:0007744\|PDB:2VJ8, ECO:0007744\|PDB:3B7R, ECO:0007744\|PDB:3B7S, ECO:0007744\|PDB:3B7T, ECO:0007744\|PDB:3B7U, ECO:0007744\|PDB:3CHO, ECO:0007744\|PDB:3CHP, ECO:0007744\|PDB:3CHQ, ECO:0007744\|PDB:3CHR, ECO:0007744\|PDB:3CHS, ECO:0007744\|PDB:3FH5, ECO:0007744\|PDB:3FH7, ECO:0007744\|PDB:3FH8, ECO:0007744\|PDB:3FHE, ECO:0007744\|PDB:3FTS, ECO:0007744\|PDB:3FTU, ECO:0007744\|PDB:3FTV, ECO:0007744\|PDB:3FTW, ECO:0007744\|PDB:3FTX, ECO:0007744\|PDB:3FTY, ECO:0007744\|PDB:3FTZ, ECO:0007744\|PDB:3FU0, ECO:0007744\|PDB:3FU3, ECO:0007744\|PDB:3FU5, ECO:0007744\|PDB:3FU6, ECO:0007744\|PDB:3FUD, ECO:0007744\|PDB:3FUE, ECO:0007744\|PDB:3FUF, ECO:0007744\|PDB:3FUH, ECO:0007744\|PDB:3FUI, ECO:0007744\|PDB:3FUJ, ECO:0007744\|PDB:3FUK, ECO:0007744\|PDB:3FUL, ECO:0007744\|PDB:3FUM, ECO:0007744\|PDB:3FUN, ECO:0007744\|PDB:3U9W, ECO:0007744\|PDB:4DPR, ECO:0007744\|PDB:4L2L, ECO:0007744\|PDB:4MKT, ECO:0007744\|PDB:4MS6, ECO:0007744\|PDB:5AEN

Chain	Residue	Details
X	GLU318

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Pro-Gly-Pro binding => ECO:0000269\|PubMed:24591641

Chain	Residue	Details
X	GLU271
X	GLY562

site_id	SWS_FT_FI7
Number of Residues	1
Details	SITE: Essential for epoxide hydrolase activity, but not for aminopeptidase activity => ECO:0000269\|PubMed:11917124

Chain	Residue	Details
X	ASP375

site_id	SWS_FT_FI8
Number of Residues	1
Details	SITE: Covalently modified during suicide inhibition by leukotrienes => ECO:0000269\|PubMed:7667299

Chain	Residue	Details
X	TYR378

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
X	LYS72
X	LYS336
X	LYS413
X	LYS572

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:9395533

Chain	Residue	Details
X	SER415

Catalytic Information from CSA

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

Chain	Residue	Details
X	TYR383
X	GLU296
X	GLU271

site_id	MCSA1
Number of Residues	7
Details	M-CSA 166

Chain	Residue	Details
X	GLU271	electrostatic stabiliser, hydrogen bond acceptor, nucleofuge, nucleophile
X	HIS295	metal ligand
X	GLU296	electrostatic stabiliser
X	HIS299	metal ligand
X	GLU318	metal ligand
X	ASP375	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
X	TYR383	electrostatic stabiliser

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