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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

227561

PDB entries from 2024-11-20

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