eF-site ID 4uir-AB PDB Code 4uir Chain A, B click to enlarge Title Structure of oleate hydratase from Elizabethkingia meningoseptica Classification LYASE Compound OLEATE HYDRATASE Source Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) (OLHYD_ELIME) Sequence A:  NPITSKFDKVLNASSEYGHVNHEPDSSKEQQRNTPQKSMP FSDQIGNYQRNKGIPVQSYDNSKIYIIGSGIAGMSAAYYF IRDGHVPAKNITFLEQLHIDGGSLDGAGNPTDGYIIRGGR EMDMTYENLWDMFQDIPALEMPAPYSVLDEYRLINDNDSN YSKARLINNKGEIKDFSKFGLNKMDQLAIIRLLLKNKEEL DDLTIEDYFSESFLKSNFWTFWRTMFAFENWHSLLELKLY MHRFLHAIDGLNDLSSLVFPKYNQYDTFVTPLRKFLQEKG VNIHLNTLVKDLDIHINTEGKVVEGIITEQDGKEVKIPVG KNDYVIVTTGSMTEDTFYGNNKTAPIIGIDNSTSGQSAGW KLWKNLAAKSEIFGKPEKFCSNIEKSAWESATLTCKPSAL IDKLKEYSVNDPYSGKTVTGGIITITDSNWLMSFTCNRQP HFPEQPDDVLVLWVYALFMDKEGNYIKKTMLECTGDEILA ELCYHLGIEDQLENVQKNTIVRTAFMPYITSMFMPRAKGD RPRVVPEGCKNLGLVGQFVETNNDVVFTMESSVRTARIAV YKLLNLNKQVPDINPLQYDIRHLLKAAKTLNDDKPFVGEG LLRKVLKGTYFEHVLPAGEEHESFIAEHVNKFREWVKGIR G B:  NPITSKFDKVLNASSEYGHVNHEPDSSKEQQRNTPQKSMP FSDQIGNYQRNKGIPVQSYDNSKIYIIGSGIAGMSAAYYF IRDGHVPAKNITFLEQLHIDGGSLDGAGNPTDGYIIREMD MTYENLWDMFQDIPALEMPAPYSVLDEYRLINDNDSNYSK ARLINNKGEIKDFSKFGLNKMDQLAIIRLLLKNKEELDDL TIEDYFSESFLKSNFWTFWRTMFAFENWHSLLELKLYMHR FLHAIDGLNDLSSLVFPKYNQYDTFVTPLRKFLQEKGVNI HLNTLVKDLDIHINTEGKVVEGIITEQDGKEVKIPVGKND YVIVTTGSMTEDTFYGNNKTAPIIGIDNSTSGQSAGWKLW KNLAAKSEIFGKPEKFCSNIEKSAWESATLTCKPSALIDK LKEYSVNDPYSGKTVTGGIITITDSNWLMSFTCNRQPHFP EQPDDVLVLWVYALFMDKEGNYIKKTMLECTGDEILAELC YHLGIEDQLENVQKNTIVRTAFMPYITSMFMPRAKGDRPR VVPEGCKNLGLVGQFVETNNDVVFTMESSVRTARIAVYKL LNLNKQVPDINPLQYDIRHLLKAAKTLNDDKPFVGEGLLR KVLKGTYFEHVLPAGAAEEESFIAEHVNKFREWV Description Functional site 1) chain A residue 68 type sequence I description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 2) chain A residue 69 type sequence G description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 3) chain A residue 71 type sequence G description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 4) chain A residue 72 type sequence I description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 5) chain A residue 73 type sequence A description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 6) chain A residue 96 type sequence E description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 7) chain A residue 97 type sequence Q description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 8) chain A residue 98 type sequence L description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 9) chain A residue 103 type sequence G description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 10) chain A residue 104 type sequence S description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 11) chain A residue 105 type sequence L description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 12) chain A residue 118 type sequence R description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 13) chain A residue 119 type sequence G description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 14) chain A residue 120 type sequence G description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 15) chain A residue 121 type sequence R description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 16) chain A residue 122 type sequence E description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 17) chain A residue 127 type sequence Y description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 18) chain A residue 290 type sequence V description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 19) chain A residue 329 type sequence T description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 20) chain A residue 332 type sequence S description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 21) chain A residue 334 type sequence T description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 22) chain A residue 363 type sequence L description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 23) chain A residue 510 type sequence I description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 24) chain A residue 537 type sequence G description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 25) chain A residue 538 type sequence Q description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 26) chain A residue 548 type sequence F description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 27) chain A residue 549 type sequence T description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 28) chain A residue 553 type sequence S description BINDING SITE FOR RESIDUE FAD A 701 source : AC1 29) chain B residue 599 type sequence G description BINDING SITE FOR RESIDUE PO4 B 1642 source : AC2 30) chain B residue 600 type sequence E description BINDING SITE FOR RESIDUE PO4 B 1642 source : AC2 31) chain B residue 601 type sequence G description BINDING SITE FOR RESIDUE PO4 B 1642 source : AC2 32) chain B residue 602 type sequence L description BINDING SITE FOR RESIDUE PO4 B 1642 source : AC2 33) chain A residue 250 type sequence D description BINDING SITE FOR RESIDUE NA A 1648 source : AC3 34) chain A residue 253 type sequence N description BINDING SITE FOR RESIDUE NA A 1648 source : AC3 35) chain B residue 250 type sequence D description BINDING SITE FOR RESIDUE NA B 1643 source : AC4 36) chain B residue 253 type sequence N description BINDING SITE FOR RESIDUE NA B 1643 source : AC4 37) chain A residue 120 type sequence G description BINDING SITE FOR RESIDUE P6G A 1649 source : AC5 38) chain A residue 122 type sequence E description BINDING SITE FOR RESIDUE P6G A 1649 source : AC5 39) chain A residue 226 type sequence M description BINDING SITE FOR RESIDUE P6G A 1649 source : AC5 40) chain A residue 227 type sequence F description BINDING SITE FOR RESIDUE P6G A 1649 source : AC5 41) chain A residue 241 type sequence Y description BINDING SITE FOR RESIDUE P6G A 1649 source : AC5 42) chain A residue 245 type sequence F description BINDING SITE FOR RESIDUE P6G A 1649 source : AC5 43) chain A residue 258 type sequence L description BINDING SITE FOR RESIDUE P6G A 1649 source : AC5 44) chain A residue 438 type sequence N description BINDING SITE FOR RESIDUE P6G A 1649 source : AC5 45) chain A residue 548 type sequence F description BINDING SITE FOR RESIDUE P6G A 1649 source : AC5 46) chain A residue 241 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:26077980 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 241 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:26077980 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 73 type BINDING sequence A description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 49) chain A residue 96 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 50) chain A residue 97 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 51) chain A residue 104 type BINDING sequence S description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 52) chain A residue 122 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 53) chain A residue 127 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 54) chain A residue 290 type BINDING sequence V description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 55) chain A residue 332 type BINDING sequence S description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 56) chain A residue 549 type BINDING sequence T description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 57) chain A residue 553 type BINDING sequence S description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 58) chain B residue 73 type BINDING sequence A description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 59) chain B residue 96 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 60) chain B residue 97 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 61) chain B residue 104 type BINDING sequence S description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 62) chain B residue 122 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 63) chain B residue 127 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 64) chain B residue 290 type BINDING sequence V description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 65) chain B residue 332 type BINDING sequence S description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 66) chain B residue 549 type BINDING sequence T description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 67) chain B residue 553 type BINDING sequence S description BINDING => ECO:0000269|PubMed:26077980, ECO:0007744|PDB:4UIR source Swiss-Prot : SWS_FT_FI3 68) chain A residue 122 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:26077980 source Swiss-Prot : SWS_FT_FI1 69) chain B residue 122 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:26077980 source Swiss-Prot : SWS_FT_FI1

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