eF-site ID 4c4x-AB PDB Code 4c4x Chain A, B click to enlarge Title Crystal structure of human bifunctional epoxide hydroxylase 2 complexed with C9 Classification HYDROLASE Compound BIFUNCTIONAL EPOXIDE HYDROLASE 2 Source (HYES_HUMAN) Sequence A:  SDMSHGYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSW RYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLC KEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRA VASLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAE AELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPE EPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWK WACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHL KRGHIEDCGHWTQMDKPTEVNQILIKWLDSDAR B:  PSDMSHGYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYS WRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVL CKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVR AVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVA EAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSP EEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNW KWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPH LKRGHIEDCGHWTQMDKPTEVNQILIKWLDSDAR Description Functional site 1) chain A residue 267 type sequence F description BINDING SITE FOR RESIDUE W9M A 1548 source : AC1 2) chain A residue 335 type sequence D description BINDING SITE FOR RESIDUE W9M A 1548 source : AC1 3) chain A residue 383 type sequence Y description BINDING SITE FOR RESIDUE W9M A 1548 source : AC1 4) chain A residue 408 type sequence L description BINDING SITE FOR RESIDUE W9M A 1548 source : AC1 5) chain A residue 419 type sequence M description BINDING SITE FOR RESIDUE W9M A 1548 source : AC1 6) chain A residue 466 type sequence Y description BINDING SITE FOR RESIDUE W9M A 1548 source : AC1 7) chain A residue 498 type sequence V description BINDING SITE FOR RESIDUE W9M A 1548 source : AC1 8) chain A residue 524 type sequence H description BINDING SITE FOR RESIDUE W9M A 1548 source : AC1 9) chain B residue 267 type sequence F description BINDING SITE FOR RESIDUE W9M B 1548 source : AC2 10) chain B residue 335 type sequence D description BINDING SITE FOR RESIDUE W9M B 1548 source : AC2 11) chain B residue 383 type sequence Y description BINDING SITE FOR RESIDUE W9M B 1548 source : AC2 12) chain B residue 408 type sequence L description BINDING SITE FOR RESIDUE W9M B 1548 source : AC2 13) chain B residue 419 type sequence M description BINDING SITE FOR RESIDUE W9M B 1548 source : AC2 14) chain B residue 466 type sequence Y description BINDING SITE FOR RESIDUE W9M B 1548 source : AC2 15) chain B residue 498 type sequence V description BINDING SITE FOR RESIDUE W9M B 1548 source : AC2 16) chain B residue 524 type sequence H description BINDING SITE FOR RESIDUE W9M B 1548 source : AC2 17) 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 18) chain B 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 19) chain A residue 370 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P34914 source Swiss-Prot : SWS_FT_FI5 20) chain B residue 370 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P34914 source Swiss-Prot : SWS_FT_FI5 21) chain A residue 421 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P34914 source Swiss-Prot : SWS_FT_FI6 22) chain A residue 455 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P34914 source Swiss-Prot : SWS_FT_FI6 23) chain B residue 421 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P34914 source Swiss-Prot : SWS_FT_FI6 24) chain B residue 455 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P34914 source Swiss-Prot : SWS_FT_FI6 25) 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_FI7 26) chain B 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_FI7 27) 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_FI4 28) chain B 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_FI4 29) 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 30) chain B 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 31) 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 32) chain B 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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