eF-site ID 2h6u-ABCDEFGH PDB Code 2h6u Chain A, B, C, D, E, F, G, H click to enlarge Title Crystal structure of 5-hydroxyisourate hydrolase (formerly known as TRP, transthyretin related protein) Classification HYDROLASE Compound 5-HYDROXYISOURATE HYDROLASE (FORMERLY KNOWN AS TRP, TRANSTHYRETIN RELATED PROTEIN) Source (Q0P422_BRARE) Sequence A:  LSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTG ITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCF YPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS B:  LSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTG ITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCF YPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS C:  LSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTG ITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCF YPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS D:  LSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTG ITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCF YPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS E:  LSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTG ITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCF YPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS F:  LSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTG ITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCF YPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS G:  LSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTG ITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCF YPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS H:  LSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTG ITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCF YPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS Description Functional site 1) chain A residue 12 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 2) chain A residue 52 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 3) chain A residue 116 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 4) chain B residue 12 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 5) chain B residue 52 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 6) chain B residue 116 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 7) chain C residue 12 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 8) chain C residue 52 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 9) chain C residue 116 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 10) chain D residue 12 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 11) chain D residue 52 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 12) chain D residue 116 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 13) chain E residue 12 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 14) chain E residue 52 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 15) chain E residue 116 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 16) chain F residue 12 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 17) chain F residue 52 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 18) chain F residue 116 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 19) chain G residue 12 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 20) chain G residue 52 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 21) chain G residue 116 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 22) chain H residue 12 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 23) chain H residue 52 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 24) chain H residue 116 type BINDING sequence Y description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 12-27 type prosite sequence HVLNIAQGVPGANMTI description TRANSTHYRETIN_1 Transthyretin signature 1. HVLNiaqGvPGanMtI source prosite : PS00768

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