eF-site ID 2y0f-ABCD PDB Code 2y0f Chain A, B, C, D click to enlarge Title STRUCTURE OF GCPE (IspG) FROM THERMUS THERMOPHILUS HB27 Classification OXIDOREDUCTASE Compound 4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE Source (ISPG_THET2) Sequence A:  MRRPTPTVYVGRVPIGGAHPIAVQSMTNTPTRDVEATTAQ VLELHRAGSEIVRLTVNDEEAAKAVPEIKRRLLAEGVEVP LVGDFHFNGHLLLRKYPKMAEALDKFRINPGTLGRGRHKD EHFAEMIRIAMDLGKPVRIGANWGSLDPALLTELMDRNAS RPEPKSAHEVVLEALVESAVRAYEAALEMGLGEDKLVLSA KVSKARDLVWVYRELARRTQAPLHLGLTEAGMGVKGIVAS AAALAPLLLEGIGDTIRVSLTPSPKEPRTKEVEVAQEILQ ALGLRAFAPEVTSCPGCGRTTSTFFQELAEEVSRRLKERL PEWRARYPGVEELKVAVMGCVVNGPGESKHAHIGISLPGA GEEPKAPVYADGKLLTILKGEGIAEEFLRLVEDYVKTRFA PKA B:  MRRPTPTVYVGRVPIGGAHPIAVQSMTNTPTRDVEATTAQ VLELHRAGSEIVRLTVNDEEAAKAVPEIKRRLLAEGVEVP LVGDFHFNGHLLLRKYPKMAEALDKFRINPGEHFAEMIRI AMDLGKPVRIGANWGSLDPALLTELMDRNASRPEPKSAHE VVLEALVESAVRAYEAALEMGLGEDKLVLSAKVSKARDLV WVYRELARRTQAPLHLGLTEAGMGVKGIVASAAALAPLLL EGIGDTIRVSLTPSPKEPRTKEVEVAQEILQALGLRAFAP EVTSCPGCGRTTSTFFQELAEEVSRRLKERLPEWRARYPG VEELKVAVMGCVVNGPGESKHAHIGISLPGAGEEPKAPVY ADGKLLTILKGEGIAEEFLRLVEDYVKTRFAPKA C:  MRRPTPTVYVGRVPIGGAHPIAVQSMTNTPTRDVEATTAQ VLELHRAGSEIVRLTVNDEEAAKAVPEIKRRLLAEGVEVP LVGDFHFNGHLLLRKYPKMAEALDKFRINPGTLHFAEMIR IAMDLGKPVRIGANWGSLDPALLTELMDRNASRPEPKSAH EVVLEALVESAVRAYEAALEMGLGEDKLVLSAKVSKARDL VWVYRELARRTQAPLHLGLTEAGMGVKGIVASAAALAPLL LEGIGDTIRVSLTPEPRTKEVEVAQEILQALGLRAFAPEV TSCPGCGRTTSTFFQELAEEVSRRLKERLPEWRARYPGVE ELKVAVMGCVVNGPGESKHAHIGISLPGAGEEPKAPVYAD GKLLTILKGEGIAEEFLRLVEDYVKTRFAPKA D:  MRRPTPTVYVGRVPIGGAHPIAVQSMTNTPTRDVEATTAQ VLELHRAGSEIVRLTVNDEEAAKAVPEIKRRLLAEGVEVP LVGDFHFNGHLLLRKYPKMAEALDKFRINPEHFAEMIRIA MDLGKPVRIGANWGSLDPALLTELMDRNASRPEPKSAHEV VLEALVESAVRAYEAALEMGLGEDKLVLSAKVSKARDLVW VYRELARRTQAPLHLGLTEAGMGVKGIVASAAALAPLLLE GIGDTIRVSLTPSPKEPRTKEVEVAQEILQALGLRAFAPE VTSCPGCGRTTSTFFQELAEEVSRRLKERLPEWRARYPGV EELKVAVMGCVVNGPGESKHAHIGISLPGAGEEPKAPVYA DGKLLTILKGEGIAEEFLRLVEDYVKTRFAPKA Description Functional site 1) chain A residue 297 type sequence C description BINDING SITE FOR RESIDUE SF4 A 501 source : AC1 2) chain A residue 298 type sequence P description BINDING SITE FOR RESIDUE SF4 A 501 source : AC1 3) chain A residue 299 type sequence G description BINDING SITE FOR RESIDUE SF4 A 501 source : AC1 4) chain A residue 300 type sequence C description BINDING SITE FOR RESIDUE SF4 A 501 source : AC1 5) chain A residue 342 type sequence G description BINDING SITE FOR RESIDUE SF4 A 501 source : AC1 6) chain A residue 343 type sequence C description BINDING SITE FOR RESIDUE SF4 A 501 source : AC1 7) chain A residue 346 type sequence N description BINDING SITE FOR RESIDUE SF4 A 501 source : AC1 8) chain A residue 350 type sequence E description BINDING SITE FOR RESIDUE SF4 A 501 source : AC1 9) chain B residue 158 type sequence M description BINDING SITE FOR RESIDUE SF4 A 501 source : AC1 10) chain A residue 158 type sequence M description BINDING SITE FOR RESIDUE SF4 B 501 source : AC2 11) chain B residue 297 type sequence C description BINDING SITE FOR RESIDUE SF4 B 501 source : AC2 12) chain B residue 300 type sequence C description BINDING SITE FOR RESIDUE SF4 B 501 source : AC2 13) chain B residue 343 type sequence C description BINDING SITE FOR RESIDUE SF4 B 501 source : AC2 14) chain B residue 346 type sequence N description BINDING SITE FOR RESIDUE SF4 B 501 source : AC2 15) chain B residue 350 type sequence E description BINDING SITE FOR RESIDUE SF4 B 501 source : AC2 16) chain C residue 297 type sequence C description BINDING SITE FOR RESIDUE SF4 C 501 source : AC3 17) chain C residue 298 type sequence P description BINDING SITE FOR RESIDUE SF4 C 501 source : AC3 18) chain C residue 300 type sequence C description BINDING SITE FOR RESIDUE SF4 C 501 source : AC3 19) chain C residue 342 type sequence G description BINDING SITE FOR RESIDUE SF4 C 501 source : AC3 20) chain C residue 343 type sequence C description BINDING SITE FOR RESIDUE SF4 C 501 source : AC3 21) chain C residue 346 type sequence N description BINDING SITE FOR RESIDUE SF4 C 501 source : AC3 22) chain C residue 350 type sequence E description BINDING SITE FOR RESIDUE SF4 C 501 source : AC3 23) chain D residue 158 type sequence M description BINDING SITE FOR RESIDUE SF4 C 501 source : AC3 24) chain C residue 158 type sequence M description BINDING SITE FOR RESIDUE SF4 D 501 source : AC4 25) chain D residue 297 type sequence C description BINDING SITE FOR RESIDUE SF4 D 501 source : AC4 26) chain D residue 298 type sequence P description BINDING SITE FOR RESIDUE SF4 D 501 source : AC4 27) chain D residue 299 type sequence G description BINDING SITE FOR RESIDUE SF4 D 501 source : AC4 28) chain D residue 300 type sequence C description BINDING SITE FOR RESIDUE SF4 D 501 source : AC4 29) chain D residue 342 type sequence G description BINDING SITE FOR RESIDUE SF4 D 501 source : AC4 30) chain D residue 343 type sequence C description BINDING SITE FOR RESIDUE SF4 D 501 source : AC4 31) chain D residue 346 type sequence N description BINDING SITE FOR RESIDUE SF4 D 501 source : AC4 32) chain D residue 350 type sequence E description BINDING SITE FOR RESIDUE SF4 D 501 source : AC4 33) chain A residue 297 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1 34) chain C residue 300 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1 35) chain C residue 343 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1 36) chain C residue 350 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1 37) chain D residue 297 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1 38) chain D residue 300 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1 39) chain D residue 343 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1 40) chain D residue 350 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 300 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 343 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 350 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1 44) chain B residue 297 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1 45) chain B residue 300 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 343 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 350 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1 48) chain C residue 297 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158 source Swiss-Prot : SWS_FT_FI1

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