6O5H

The effect of modifier structure on the activation of leukotriene A4 hydrolase aminopeptidase activity.

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
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	0016787	molecular_function	hydrolase activity
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	0016787	molecular_function	hydrolase activity
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	13
Details	binding site for residue LNJ A 701

Chain	Residue
A	GLN134
A	VAL367
A	LEU369
A	TYR378
A	VAL381
A	GLN136
A	ALA137
A	TYR267
A	TRP311
A	PHE314
A	PHE362
A	LYS364
A	LEU365

---

site_id	AC2
Number of Residues	5
Details	binding site for residue ZN A 702

Chain	Residue
A	HIS295
A	HIS299
A	GLU318
A	TYR383
A	HOH856

---

site_id	AC3
Number of Residues	13
Details	binding site for residue LNJ B 701

Chain	Residue
B	GLN136
B	ALA137
B	TYR267
B	TRP311
B	PHE314
B	LYS364
B	LEU365
B	VAL366
B	VAL367
B	LEU369
B	PRO374
B	TYR378
B	PRO382

---

site_id	AC4
Number of Residues	5
Details	binding site for residue ZN B 702

Chain	Residue
B	HIS295
B	HIS299
B	GLU318
B	TYR383
B	HOH860

---

site_id	AC5
Number of Residues	13
Details	binding site for residue LNJ C 701

Chain	Residue
C	GLN134
C	GLN136
C	ALA137
C	TYR267
C	TRP311
C	PHE314
C	PHE362
C	LYS364
C	LEU365
C	VAL367
C	ALA377
C	TYR378
C	PRO382

---

site_id	AC6
Number of Residues	4
Details	binding site for residue ZN C 702

Chain	Residue
C	HIS295
C	HIS299
C	GLU318
C	TYR383

---

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
A	GLN134
A	PRO266
A	ARG563
B	GLN134
B	PRO266
B	ARG563
C	GLN134
C	PRO266
C	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
A	HIS295
A	HIS299
B	HIS295
B	HIS299
C	HIS295
C	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
A	GLU318
B	GLU318
C	GLU318

---

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

Chain	Residue	Details
A	GLU271
A	GLY562
B	GLU271
B	GLY562
C	GLU271
C	GLY562

---

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
A	ASP375
B	ASP375
C	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	LYS72
C	LYS336
C	LYS413
C	LYS572
A	LYS336
A	LYS413
A	LYS572
B	LYS72
B	LYS336
B	LYS413
B	LYS572
C	LYS72

---

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	GLU271	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	GLU271	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
B	TYR383	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	7
Details	M-CSA 166

Chain	Residue	Details
C	GLU271	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

---