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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8TWX

Synthesis and Evaluation of Diaryl Ether Modulators of the Leukotriene A4 Hydrolase Aminopeptidase Activity

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 Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:11675384, ECO:0000305|PubMed:12207002, ECO:0000305|PubMed:24591641, ECO:0007744|PDB:1H19
ChainResidueDetails
AGLU296
BGLU296
CGLU296
site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:11675384, ECO:0000305|PubMed:12207002, ECO:0000305|PubMed:24591641, ECO:0007744|PDB:1H19
ChainResidueDetails
ATYR383
BTYR383
CTYR383
site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:18804029
ChainResidueDetails
AGLN134
APRO266
AARG563
BGLN134
BPRO266
BARG563
CGLN134
CPRO266
CARG563
site_idSWS_FT_FI4
Number of Residues6
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
BHIS295
BHIS299
CHIS295
CHIS299
site_idSWS_FT_FI5
Number of Residues3
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
BGLU318
CGLU318
site_idSWS_FT_FI6
Number of Residues6
DetailsSITE: Pro-Gly-Pro binding => ECO:0000269|PubMed:24591641
ChainResidueDetails
AGLU271
AGLY562
BGLU271
BGLY562
CGLU271
CGLY562
site_idSWS_FT_FI7
Number of Residues3
DetailsSITE: Essential for epoxide hydrolase activity, but not for aminopeptidase activity => ECO:0000269|PubMed:11917124
ChainResidueDetails
AASP375
BASP375
CASP375
site_idSWS_FT_FI8
Number of Residues3
DetailsSITE: Covalently modified during suicide inhibition by leukotrienes => ECO:0000269|PubMed:7667299
ChainResidueDetails
ATYR378
BTYR378
CTYR378
site_idSWS_FT_FI9
Number of Residues12
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS72
CLYS336
CLYS413
CLYS572
ALYS336
ALYS413
ALYS572
BLYS72
BLYS336
BLYS413
BLYS572
CLYS72
site_idSWS_FT_FI10
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9395533
ChainResidueDetails
ASER415
BSER415
CSER415
Catalytic Information from CSA
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
site_idMCSA2
Number of Residues7
DetailsM-CSA 166
ChainResidueDetails
BGLU271electrostatic stabiliser, hydrogen bond acceptor, nucleofuge, nucleophile
BHIS295metal ligand
BGLU296electrostatic stabiliser
BHIS299metal ligand
BGLU318metal ligand
BASP375hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BTYR383electrostatic stabiliser
site_idMCSA3
Number of Residues7
DetailsM-CSA 166
ChainResidueDetails
CGLU271electrostatic stabiliser, hydrogen bond acceptor, nucleofuge, nucleophile
CHIS295metal ligand
CGLU296electrostatic stabiliser
CHIS299metal ligand
CGLU318metal ligand
CASP375hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
CTYR383electrostatic stabiliser

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PDB entries from 2024-08-28

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