Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3U9W

Structure of human Leukotriene A4 hydrolase in complex with inhibitor sc57461A

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 2001

Chain	Residue
A	HIS1295
A	HIS1299
A	GLU1318
A	28P7001

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE YB A 2002

Chain	Residue
A	HOH8118
A	ACT1
A	ASP1047
A	ASP1481
A	HOH8062
A	HOH8066

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 2007

Chain	Residue
A	ASP1058
A	ARG1078
A	SER1084

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 2008

Chain	Residue
A	PRO1216
A	PRO1513
A	GLY1515

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE IMD A 2009

Chain	Residue
A	GLY1344
A	GLY1347
A	GLU1348
A	GLU1501
A	ALA1504
A	GLN1508

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE IMD A 2010

Chain	Residue
A	SER1288
A	LEU1289
A	SER1496
A	HIS1497
A	ASN1500
A	ASN1531
A	HOH8436

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 2011

Chain	Residue
A	PHE1029
A	ARG1032
A	TRP1117
A	LEU1118
A	PRO1120
A	HOH8236
A	HOH8548
A	HOH8552

site_id	AC8
Number of Residues	18
Details	BINDING SITE FOR RESIDUE 28P A 7001

Chain	Residue
A	GLN1136
A	TYR1267
A	GLY1269
A	MET1270
A	GLU1271
A	HIS1295
A	GLU1296
A	HIS1299
A	TRP1311
A	PHE1314
A	GLU1318
A	VAL1367
A	PRO1374
A	ALA1377
A	TYR1378
A	PRO1382
A	TYR1383
A	ZN2001

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ACT A 1

Chain	Residue
A	ASP1047
A	ASN1048
A	ARG1174
A	LYS1479
A	ASP1481
A	YB2002
A	HOH8010
A	HOH8062
A	HOH8118
A	HOH8615

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE YB A 1611

Chain	Residue
A	YB2
A	ASP1426
A	HOH8913
A	HOH8914
A	HOH8915
A	HOH8920

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE YB A 2

Chain	Residue
A	YB7
A	ASP1426
A	ASP1610
A	YB1611
A	HOH8908
A	HOH8914
A	HOH8915
A	HOH8929

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE YB A 3

Chain	Residue
A	ASP1175
A	HOH8925
A	HOH8927
A	HOH8928

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE YB A 4

Chain	Residue
A	IMD186
A	ARG1024
A	GLU1182
A	HOH8226
A	HOH8421

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE YB A 5

Chain	Residue
A	GLU1070
A	HOH8727

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE YB A 6

Chain	Residue
A	GLU1182
A	GLU1590

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE YB A 7

Chain	Residue
A	YB2
A	ASP1426
A	ASP1610
A	HOH8908
A	HOH8914

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE IMD A 186

Chain	Residue
A	CYS1025
A	GLU1159
A	ILE1188
A	HOH8226
A	HOH8380
A	YB4
A	ARG1024

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
A	VAL1292-TRP1301

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
A	GLU1296

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
A	TYR1383

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

Chain	Residue	Details
A	GLN1134
A	PRO1266
A	ARG1563

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
A	HIS1295
A	HIS1299

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
A	GLU1318

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

Chain	Residue	Details
A	GLU1271
A	GLY1562

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
A	ASP1375

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
A	TYR1378

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

Chain	Residue	Details
A	LYS1072
A	LYS1336
A	LYS1413
A	LYS1572

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

Chain	Residue	Details
A	SER1415

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 166

Chain	Residue	Details
A	GLU1271	electrostatic stabiliser, hydrogen bond acceptor, nucleofuge, nucleophile
A	HIS1295	metal ligand
A	GLU1296	electrostatic stabiliser
A	HIS1299	metal ligand
A	GLU1318	metal ligand
A	ASP1375	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	TYR1383	electrostatic stabiliser

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