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3FUH

Leukotriene A4 hydrolase in complex with fragment 5-hydroxyindole and bestatin

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0004177molecular_functionaminopeptidase activity
A0004301molecular_functionepoxide hydrolase activity
A0004463molecular_functionleukotriene-A4 hydrolase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0006629biological_processlipid metabolic process
A0006691biological_processleukotriene metabolic process
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0010043biological_processresponse to zinc ion
A0019370biological_processleukotriene biosynthetic process
A0019538biological_processprotein metabolic process
A0043171biological_processpeptide catabolic process
A0043434biological_processresponse to peptide hormone
A0045148molecular_functiontripeptide aminopeptidase activity
A0046872molecular_functionmetal ion binding
A0060509biological_processtype I pneumocyte differentiation
A0070006molecular_functionmetalloaminopeptidase activity
A0070062cellular_componentextracellular exosome
A1904724cellular_componenttertiary granule lumen
A1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 701
ChainResidue
AHIS295
AHIS299
AGLU318
ABES720

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE YB A 702
ChainResidue
AHOH1214
AASP47
AASP481
AHOH689
AHOH1035
AHOH1078

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE YB A 703
ChainResidue
AASP175

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE YB A 704
ChainResidue
AHOH1108

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 5H1 A 710
ChainResidue
ATRP311
APHE314
APRO374
AALA377
ABES720
AHOH1213
AHOH1234

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE BES A 720
ChainResidue
AGLN134
AGLN136
ATYR267
AGLY268
AGLY269
AMET270
AGLU271
AHIS295
AGLU296
AHIS299
APHE314
AGLU318
ATYR378
ATYR383
AHOH647
AZN701
A5H1710
AHOH818
AHOH1067

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IMD A 801
ChainResidue
AGLY344
AGLY347
AGLU348
AGLU501
AALA504
AGLN508

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHEISHSW
ChainResidueDetails
AVAL292-TRP301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:11675384, ECO:0000305|PubMed:12207002, ECO:0000305|PubMed:24591641, ECO:0007744|PDB:1H19
ChainResidueDetails
AGLU296

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:11675384, ECO:0000305|PubMed:12207002, ECO:0000305|PubMed:24591641, ECO:0007744|PDB:1H19
ChainResidueDetails
ATYR383

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18804029
ChainResidueDetails
AGLN134
APRO266
AARG563

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
AHIS295
AHIS299

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: 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
ChainResidueDetails
AGLU318

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Pro-Gly-Pro binding => ECO:0000269|PubMed:24591641
ChainResidueDetails
AGLU271
AGLY562

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Essential for epoxide hydrolase activity, but not for aminopeptidase activity => ECO:0000269|PubMed:11917124
ChainResidueDetails
AASP375

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Covalently modified during suicide inhibition by leukotrienes => ECO:0000269|PubMed:7667299
ChainResidueDetails
ATYR378

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS72
ALYS336
ALYS413
ALYS572

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9395533
ChainResidueDetails
ASER415

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1h19
ChainResidueDetails
ATYR383
AGLU296
AGLU271

site_idMCSA1
Number of Residues7
DetailsM-CSA 166
ChainResidueDetails
AGLU271electrostatic stabiliser, hydrogen bond acceptor, nucleofuge, nucleophile
AHIS295metal ligand
AGLU296electrostatic stabiliser
AHIS299metal ligand
AGLU318metal ligand
AASP375hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ATYR383electrostatic stabiliser

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PDB entries from 2024-11-06

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