eF-site ID 5alw-A PDB Code 5alw Chain A click to enlarge Title ligand complex structure of soluble epoxide hydrolase Classification HYDROLASE Compound BIFUNCTIONAL EPOXIDE HYDROLASE 2 Source Homo sapiens (Human) (HYES_HUMAN) Sequence A:  TLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAF QKGGPEGATTRLMKGEITLSQWIPLMEENCRKCSETAKVC LPKNFSIKEIFDKAISARKINRPMLQAALMLRKKGFTTAI LTNTWLDDRAERDGLAQLMCELKMHFDFLIESCQVGMVKP EPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTI LVQDTDTALKELEKVTGIQLLNTPAPLPTSCNPSDMSHGY VTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPAL AQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFL DKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTP FIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNL SRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRM VTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLG RKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIED CGHWTQMDKPTEVNQILIKWLDSDAR Description Functional site 1) chain A residue 335 type sequence D description BINDING SITE FOR RESIDUE SO4 A 1548 source : AC1 2) chain A residue 336 type sequence W description BINDING SITE FOR RESIDUE SO4 A 1548 source : AC1 3) chain A residue 339 type sequence M description BINDING SITE FOR RESIDUE SO4 A 1548 source : AC1 4) chain A residue 228 type sequence L description BINDING SITE FOR RESIDUE DMS A 1549 source : AC2 5) chain A residue 440 type sequence R description BINDING SITE FOR RESIDUE DMS A 1549 source : AC2 6) chain A residue 441 type sequence M description BINDING SITE FOR RESIDUE DMS A 1549 source : AC2 7) chain A residue 442 type sequence V description BINDING SITE FOR RESIDUE DMS A 1549 source : AC2 8) chain A residue 443 type sequence T description BINDING SITE FOR RESIDUE DMS A 1549 source : AC2 9) chain A residue 144 type sequence K description BINDING SITE FOR RESIDUE DMS A 1550 source : AC3 10) chain A residue 147 type sequence F description BINDING SITE FOR RESIDUE DMS A 1550 source : AC3 11) chain A residue 149 type sequence F description BINDING SITE FOR RESIDUE DMS A 1550 source : AC3 12) chain A residue 150 type sequence L description BINDING SITE FOR RESIDUE DMS A 1550 source : AC3 13) chain A residue 267 type sequence F description BINDING SITE FOR RESIDUE JQN A 1551 source : AC4 14) chain A residue 383 type sequence Y description BINDING SITE FOR RESIDUE JQN A 1551 source : AC4 15) chain A residue 387 type sequence F description BINDING SITE FOR RESIDUE JQN A 1551 source : AC4 16) chain A residue 408 type sequence L description BINDING SITE FOR RESIDUE JQN A 1551 source : AC4 17) chain A residue 419 type sequence M description BINDING SITE FOR RESIDUE JQN A 1551 source : AC4 18) chain A residue 428 type sequence L description BINDING SITE FOR RESIDUE JQN A 1551 source : AC4 19) chain A residue 496 type sequence D description BINDING SITE FOR RESIDUE JQN A 1551 source : AC4 20) chain A residue 497 type sequence F description BINDING SITE FOR RESIDUE JQN A 1551 source : AC4 21) chain A residue 498 type sequence V description BINDING SITE FOR RESIDUE JQN A 1551 source : AC4 22) chain A residue 524 type sequence H description BINDING SITE FOR RESIDUE JQN A 1551 source : AC4 23) chain A residue 525 type sequence W description BINDING SITE FOR RESIDUE JQN A 1551 source : AC4 24) chain A residue 43 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 25) chain A residue 55 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P34914 source Swiss-Prot : SWS_FT_FI7 26) chain A residue 421 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P34914 source Swiss-Prot : SWS_FT_FI7 27) chain A residue 455 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P34914 source Swiss-Prot : SWS_FT_FI7 28) chain A residue 191 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P34914 source Swiss-Prot : SWS_FT_FI8 29) chain A residue 215 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P34914 source Swiss-Prot : SWS_FT_FI8 30) chain A residue 370 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P34914 source Swiss-Prot : SWS_FT_FI9 31) chain A residue 335 type ACT_SITE sequence D description Nucleophile => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 524 type ACT_SITE sequence H description Proton acceptor => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 9 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15096040 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 11 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15096040 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 123 type BINDING sequence T description BINDING => ECO:0000269|PubMed:15096040 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 185 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15096040 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 383 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334 source Swiss-Prot : SWS_FT_FI5 38) chain A residue 522 type LIPID sequence C description S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine => ECO:0000305|PubMed:21164107 source Swiss-Prot : SWS_FT_FI10 39) chain A residue 466 type ACT_SITE sequence Y description Proton donor => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334 source Swiss-Prot : SWS_FT_FI2

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