eF-site ID 2xmh-ABCDEF PDB Code 2xmh Chain A, B, C, D, E, F click to enlarge Title The X-ray structure of CTP:inositol-1-phosphate cytidylyltransferase from Archaeoglobus fulgidus Classification TRANSFERASE Compound CTP-INOSITOL-1-PHOSPHATE CYTIDYLYLTRANSFERASE Source (O29976_ARCFU) Sequence A:  IKLMKAVILAVPKPLVRVGGCEIILRTMKLLSPHVSEFII VASRYADDIDAFLKDKGFNYKIVRHDRPEKGNGYSLLVAK NHVEDRFILTMGDHVYSQQFIEKAVRGEGVIADREPRFVD IGEATKIRVEDGRVAKIGKDLREFDCVDTGFFVLDDSIFE HAEKLRDREEIPLSEIVKLARLPVTYVDGELWMDVD B:  IKLMKAVILAAPKPLVRVGGCEIILRTMKLLSPHVSEFII VASRYADDIDAFLKDKGFNYKIVRHDRPEKGNGYSLLVAK NHVEDRFILTMGDHVYSQQFIEKAVRGEGVIADREPRFVD IGEATKIRVEDGRVAKIGKDLREFDCVDTGFFVLDDSIFE HAEKLRDREEIPLSEIVKLARLPVTYVDGELWMDVD C:  LMKAVILAAGLRLGGVPKPLVRVGGCEIILRTMKLLSPHV SEFIIVASRYADDIDAFLKDKGFNYKIVRHDRPEKGNGYS LLVAKNHVEDRFILTMGDHVYSQQFIEKAVRGEGVIADRE PRFVDIGEATKIRVEDGRVAKIGKDLREFDCVDTGFFVLD DSIFEHAEKLRDREEIPLSEIVKLARLPVTYVDGELWMDV D D:  IKLMKAVILAAGLGTRLGGVPKPLVRVGGCEIILRTMKLL SPHVSEFIIVASRYADDIDAFLKDKGFNYKIVRHDRPEKG NGYSLLVAKNHVEDRFILTMGDHVYSQQFIEKAVRGEGVI ADREPRFVDIGEATKIRVEDGRVAKIGKDLREFDCVDTGF FVLDDSIFEHAEKLRDREEIPLSEIVKLARLPVTYVDGEL WMDVD E:  IKLMKAVILAAGLGTRLGGVPKPLVRVGGCEIILRTMKLL SPHVSEFIIVASRYADDIDAFLKDKGFNYKIVRHDRPEKG NGYSLLVAKNHVEDRFILTMGDHVYSQQFIEKAVRGEGVI ADREPRFVDIGEATKIRVEDGRVAKIGKDLREFDCVDTGF FVLDDSIFEHAEKLRDREEIPLSEIVKLARLPVTYVDGEL WMDVD F:  IKLMKAVILAAGVPKPLVRVGGCEIILRTMKLLSPHVSEF IIVASRYADDIDAFLKDKGFNYKIVRHDRPEKGNGYSLLV AKNHVEDRFILTMGDHVYSQQFIEKAVRGEGVIADREPRF VDIGEATKIRVEDGRVAKIGKDLREFDCVDTGFFVLDDSI FEHAEKLRDREEIPLSEIVKLARLPVTYVDGELWMDVDTK Description (1)  CTP-INOSITOL-1-PHOSPHATE CYTIDYLYLTRANSFERASE Functional site 1) chain A residue 25 type sequence A description BINDING SITE FOR RESIDUE FLC A 501 source : AC1 2) chain A residue 37 type sequence K description BINDING SITE FOR RESIDUE FLC A 501 source : AC1 3) chain A residue 38 type sequence P description BINDING SITE FOR RESIDUE FLC A 501 source : AC1 4) chain A residue 68 type sequence R description BINDING SITE FOR RESIDUE FLC A 501 source : AC1 5) chain D residue 25 type sequence A description BINDING SITE FOR RESIDUE FLC D 501 source : AC2 6) chain D residue 26 type sequence A description BINDING SITE FOR RESIDUE FLC D 501 source : AC2 7) chain D residue 27 type sequence G description BINDING SITE FOR RESIDUE FLC D 501 source : AC2 8) chain D residue 28 type sequence L description BINDING SITE FOR RESIDUE FLC D 501 source : AC2 9) chain D residue 29 type sequence G description BINDING SITE FOR RESIDUE FLC D 501 source : AC2 10) chain D residue 30 type sequence T description BINDING SITE FOR RESIDUE FLC D 501 source : AC2 11) chain D residue 36 type sequence P description BINDING SITE FOR RESIDUE FLC D 501 source : AC2 12) chain D residue 37 type sequence K description BINDING SITE FOR RESIDUE FLC D 501 source : AC2 13) chain D residue 68 type sequence R description BINDING SITE FOR RESIDUE FLC D 501 source : AC2 14) chain D residue 69 type sequence Y description BINDING SITE FOR RESIDUE FLC D 501 source : AC2 15) chain D residue 92 type sequence P description BINDING SITE FOR RESIDUE FLC D 501 source : AC2 16) chain E residue 25 type sequence A description BINDING SITE FOR RESIDUE FLC E 501 source : AC3 17) chain E residue 26 type sequence A description BINDING SITE FOR RESIDUE FLC E 501 source : AC3 18) chain E residue 27 type sequence G description BINDING SITE FOR RESIDUE FLC E 501 source : AC3 19) chain E residue 28 type sequence L description BINDING SITE FOR RESIDUE FLC E 501 source : AC3 20) chain E residue 29 type sequence G description BINDING SITE FOR RESIDUE FLC E 501 source : AC3 21) chain E residue 30 type sequence T description BINDING SITE FOR RESIDUE FLC E 501 source : AC3 22) chain E residue 37 type sequence K description BINDING SITE FOR RESIDUE FLC E 501 source : AC3 23) chain E residue 68 type sequence R description BINDING SITE FOR RESIDUE FLC E 501 source : AC3 24) chain E residue 69 type sequence Y description BINDING SITE FOR RESIDUE FLC E 501 source : AC3 25) chain E residue 92 type sequence P description BINDING SITE FOR RESIDUE FLC E 501 source : AC3 26) chain A residue 24 type BINDING sequence L description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 27) chain C residue 37 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 28) chain C residue 90 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 29) chain C residue 126 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 30) chain D residue 24 type BINDING sequence L description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 31) chain D residue 37 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 32) chain D residue 90 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 33) chain D residue 126 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 34) chain E residue 24 type BINDING sequence L description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 35) chain E residue 37 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 36) chain E residue 90 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 37 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 38) chain E residue 126 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 39) chain F residue 24 type BINDING sequence L description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 40) chain F residue 37 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 41) chain F residue 90 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 42) chain F residue 126 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 90 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 44) chain A residue 126 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 45) chain B residue 24 type BINDING sequence L description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 37 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 90 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 48) chain B residue 126 type BINDING sequence E description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 49) chain C residue 24 type BINDING sequence L description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1

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