Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5NI4

Crystal structure of human LTA4H mutant E271A in complex with LTA4 (crystal form II)

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue ZN A 701

Chain	Residue
A	HIS295
A	HIS299
A	GLU318
A	DJ3705
A	HOH804

site_id	AC2
Number of Residues	6
Details	binding site for residue IMD A 702

Chain	Residue
A	GLN508
A	HOH1206
A	GLY344
A	GLY347
A	GLU348
A	GLU501

site_id	AC3
Number of Residues	7
Details	binding site for residue IMD A 703

Chain	Residue
A	GLY248
A	PRO250
A	VAL252
A	GLU412
A	SER415
A	HOH1002
A	HOH1152

site_id	AC4
Number of Residues	4
Details	binding site for residue IMD A 704

Chain	Residue
A	ASP422
A	ASP426
A	HOH1004
A	HOH1385

site_id	AC5
Number of Residues	20
Details	binding site for residue DJ3 A 705

Chain	Residue
A	GLN136
A	ALA137
A	TYR267
A	GLY268
A	GLY269
A	MET270
A	HIS295
A	GLU296
A	TRP311
A	PHE314
A	GLU318
A	VAL367
A	TYR378
A	TYR383
A	ARG563
A	ZN701
A	HOH801
A	HOH804
A	HOH810
A	HOH1145

site_id	AC6
Number of Residues	5
Details	binding site for residue ZN B 701

Chain	Residue
B	HIS295
B	HIS299
B	GLU318
B	DJ3705
B	HOH808

site_id	AC7
Number of Residues	6
Details	binding site for residue IMD B 702

Chain	Residue
B	GLY344
B	GLY347
B	GLU348
B	GLU501
B	ALA504
B	GLN508

site_id	AC8
Number of Residues	2
Details	binding site for residue IMD B 703

Chain	Residue
B	ASP422
B	ASP426

site_id	AC9
Number of Residues	10
Details	binding site for residue IMD B 704

Chain	Residue
B	GLY248
B	GLY249
B	PRO250
B	LEU305
B	VAL411
B	GLU412
B	SER415
B	HOH896
B	HOH988
B	HOH1063

site_id	AD1
Number of Residues	21
Details	binding site for residue DJ3 B 705

Chain	Residue
B	GLN136
B	ALA137
B	TYR267
B	GLY268
B	GLY269
B	HIS295
B	GLU296
B	HIS299
B	TRP311
B	PHE314
B	GLU318
B	VAL367
B	PRO374
B	TYR378
B	TYR383
B	ARG563
B	LYS565
B	ZN701
B	HOH808
B	HOH870
B	HOH1007

site_id	AD2
Number of Residues	5
Details	binding site for residue ZN C 701

Chain	Residue
C	HIS295
C	HIS299
C	GLU318
C	DJ3703
C	HOH805

site_id	AD3
Number of Residues	7
Details	binding site for residue IMD C 702

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

site_id	AD4
Number of Residues	22
Details	binding site for residue DJ3 C 703

Chain	Residue
C	ALA137
C	TYR267
C	GLY268
C	GLY269
C	MET270
C	HIS295
C	GLU296
C	TRP311
C	PHE314
C	GLU318
C	VAL367
C	PRO374
C	TYR383
C	ARG563
C	LYS565
C	ZN701
C	HOH805
C	HOH865
C	HOH1025
C	HOH1169
C	HOH1203
C	GLN136

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	VAL292-TRP301

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
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	GLU296
B	GLU296
C	GLU296

site_id	SWS_FT_FI2
Number of Residues	3
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	TYR383
B	TYR383
C	TYR383

site_id	SWS_FT_FI3
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269\|PubMed:18804029

Chain	Residue	Details
C	GLN134
C	PRO266
C	ARG563
B	GLN134
B	PRO266
B	ARG563
A	GLN134
A	PRO266
A	ARG563

site_id	SWS_FT_FI4
Number of Residues	6
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
B	HIS299
C	HIS295
C	HIS299
B	HIS295
A	HIS295
A	HIS299

site_id	SWS_FT_FI5
Number of Residues	3
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
C	GLU318
A	GLU318
B	GLU318

site_id	SWS_FT_FI6
Number of Residues	6
Details	SITE: Pro-Gly-Pro binding => ECO:0000269\|PubMed:24591641

Chain	Residue	Details
B	GLY562
C	ALA271
C	GLY562
A	GLY562
B	ALA271
A	ALA271

site_id	SWS_FT_FI7
Number of Residues	3
Details	SITE: Essential for epoxide hydrolase activity, but not for aminopeptidase activity => ECO:0000269\|PubMed:11917124

Chain	Residue	Details
B	ASP375
C	ASP375
A	ASP375

site_id	SWS_FT_FI8
Number of Residues	3
Details	SITE: Covalently modified during suicide inhibition by leukotrienes => ECO:0000269\|PubMed:7667299

Chain	Residue	Details
A	TYR378
B	TYR378
C	TYR378

site_id	SWS_FT_FI9
Number of Residues	12
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS572
B	LYS72
B	LYS336
B	LYS413
B	LYS572
C	LYS72
C	LYS336
C	LYS413
C	LYS572
A	LYS72
A	LYS336
A	LYS413

site_id	SWS_FT_FI10
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:9395533

Chain	Residue	Details
A	SER415
B	SER415
C	SER415

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 166

Chain	Residue	Details
A	ALA271	electrostatic stabiliser, hydrogen bond acceptor, nucleofuge, nucleophile
A	HIS295	metal ligand
A	GLU296	electrostatic stabiliser
A	HIS299	metal ligand
A	GLU318	metal ligand
A	ASP375	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	TYR383	electrostatic stabiliser

site_id	MCSA2
Number of Residues	7
Details	M-CSA 166

Chain	Residue	Details
B	TYR383	electrostatic stabiliser
B	ALA271	electrostatic stabiliser, hydrogen bond acceptor, nucleofuge, nucleophile
B	HIS295	metal ligand
B	GLU296	electrostatic stabiliser
B	HIS299	metal ligand
B	GLU318	metal ligand
B	ASP375	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA3
Number of Residues	7
Details	M-CSA 166

Chain	Residue	Details
C	ALA271	electrostatic stabiliser, hydrogen bond acceptor, nucleofuge, nucleophile
C	HIS295	metal ligand
C	GLU296	electrostatic stabiliser
C	HIS299	metal ligand
C	GLU318	metal ligand
C	ASP375	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	TYR383	electrostatic stabiliser

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