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3B7R

Leukotriene A4 Hydrolase Complexed with Inhibitor RB3040

Functional Information from GO Data
ChainGOidnamespacecontents
L0003723molecular_functionRNA binding
L0004177molecular_functionaminopeptidase activity
L0004301molecular_functionepoxide hydrolase activity
L0004463molecular_functionleukotriene-A4 hydrolase activity
L0005515molecular_functionprotein binding
L0005576cellular_componentextracellular region
L0005634cellular_componentnucleus
L0005654cellular_componentnucleoplasm
L0005737cellular_componentcytoplasm
L0005829cellular_componentcytosol
L0006508biological_processproteolysis
L0006629biological_processlipid metabolic process
L0006691biological_processleukotriene metabolic process
L0008233molecular_functionpeptidase activity
L0008237molecular_functionmetallopeptidase activity
L0008270molecular_functionzinc ion binding
L0010043biological_processresponse to zinc ion
L0019370biological_processleukotriene biosynthetic process
L0019538biological_processprotein metabolic process
L0043171biological_processpeptide catabolic process
L0043434biological_processresponse to peptide hormone
L0045148molecular_functiontripeptide aminopeptidase activity
L0046872molecular_functionmetal ion binding
L0060509biological_processtype I pneumocyte differentiation
L0070006molecular_functionmetalloaminopeptidase activity
L0070062cellular_componentextracellular exosome
L1904724cellular_componenttertiary granule lumen
L1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN L 701
ChainResidue
LHIS295
LHIS299
LGLU318

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE YB L 801
ChainResidue
LHOH1657
LASP47
LASP481
LHOH1444
LHOH1447
LHOH1543
LHOH1609

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE IMD L 802
ChainResidue
LGLY344
LGLY347
LGLU348
LASN351
LGLU501
LALA504
LGLN508

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE BIR L 1001
ChainResidue
LGLN136
LTYR267
LGLY268
LGLY269
LGLU271
LASN291
LHIS295
LGLU296
LHIS299
LGLU318
LTYR378
LTYR383
LARG563
LLYS565
LHOH1005
LHOH1064
LHOH1391

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHEISHSW
ChainResidueDetails
LVAL292-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
LGLU296

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
LTYR383

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18804029
ChainResidueDetails
LGLN134
LPRO266
LARG563

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
LHIS295
LHIS299

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
LGLU318

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Pro-Gly-Pro binding => ECO:0000269|PubMed:24591641
ChainResidueDetails
LGLU271
LGLY562

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Essential for epoxide hydrolase activity, but not for aminopeptidase activity => ECO:0000269|PubMed:11917124
ChainResidueDetails
LASP375

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Covalently modified during suicide inhibition by leukotrienes => ECO:0000269|PubMed:7667299
ChainResidueDetails
LTYR378

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
LLYS72
LLYS336
LLYS413
LLYS572

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9395533
ChainResidueDetails
LSER415

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1h19
ChainResidueDetails
LTYR383
LGLU296
LGLU271

site_idMCSA1
Number of Residues7
DetailsM-CSA 166
ChainResidueDetails
LGLU271electrostatic stabiliser, hydrogen bond acceptor, nucleofuge, nucleophile
LHIS295metal ligand
LGLU296electrostatic stabiliser
LHIS299metal ligand
LGLU318metal ligand
LASP375hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
LTYR383electrostatic stabiliser

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PDB entries from 2024-11-06

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