1SQM

STRUCTURE OF [R563A] LEUKOTRIENE A4 HYDROLASE

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	0016787	molecular_function	hydrolase activity
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 1001

Chain	Residue
A	HIS295
A	HIS299
A	GLU318
A	ACY3001

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE YB A 2001

Chain	Residue
A	ASP47
A	ASP481
A	HOH3187
A	HOH3300
A	HOH3382

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE IMD A 2002

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

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site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACY A 3001

Chain	Residue
A	GLY269
A	GLU271
A	HIS295
A	GLU296
A	HIS299
A	GLU318
A	TYR383
A	ZN1001

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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

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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	ILE297

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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	GLU384

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

Chain	Residue	Details
A	CYS135
A	TYR267
A	MET564

---

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	GLU296
A	SER300

---

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	GLY319

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

Chain	Residue	Details
A	ASN272
A	ALA563

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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	VAL376

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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	SER379

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

Chain	Residue	Details
A	TYR73
A	PHE337
A	PHE414
A	ASP573

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

Chain	Residue	Details
A	TYR416

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 166

Chain	Residue	Details
A	ASN272	electrostatic stabiliser, hydrogen bond acceptor, nucleofuge, nucleophile
A	GLU296	metal ligand
A	ILE297	electrostatic stabiliser
A	SER300	metal ligand
A	GLY319	metal ligand
A	VAL376	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLU384	electrostatic stabiliser

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