eF-site ID 1qcn-B PDB Code 1qcn Chain B click to enlarge Title CRYSTAL STRUCTURE OF FUMARYLACETOACETATE HYDROLASE Classification HYDROLASE Compound FUMARYLACETOACETATE HYDROLASE Source null (FAAA_MOUSE) Sequence B:  GSXSFIPVAEDSDFPIQNLPYGVFSTQSNPKPRIGVAIGD QILDLSVIKHLFTGPALSKHQHVFDETTLNNFXGLGQAAW KEARASLQNLLSASQARLRDDKELRQRAFTSQASATXHLP ATIGDYTDFYSSRQHATNVGIXFRGKENALLPNWLHLPVG YHGRASSIVVSGTPIRRPXGQXRPDNSKPPVYGACRLLDX ELEXAFFVGPGNRFGEPIPISKAHEHIFGXVLXNDWSARD IQQWEYVPLGPFLGKSFGTTISPWVVPXDALXPFVVPNPK QDPKPLPYLCHSQPYTFDINLSVSLKGEGXSQAATICRSN FKHXYWTXLQQLTHHSVNGCNLRPGDLLASGTISGSDPES FGSXLELSWKGTKAIDVGQGQTRTFLLDGDEVIITGHCQG DGYRVGFGQCAGKVLPALSP Description Functional site 1) chain B residue 626 type sequence D description BINDING SITE FOR RESIDUE CA B 1002 source : AC2 2) chain B residue 699 type sequence E description BINDING SITE FOR RESIDUE CA B 1002 source : AC2 3) chain B residue 701 type sequence E description BINDING SITE FOR RESIDUE CA B 1002 source : AC2 4) chain B residue 733 type sequence D description BINDING SITE FOR RESIDUE CA B 1002 source : AC2 5) chain B residue 499 type sequence G description BINDING SITE FOR RESIDUE NI B 1003 source : AC3 6) chain B residue 746 type sequence P description BINDING SITE FOR RESIDUE ACT A 1005 source : AC5 7) chain B residue 626 type sequence D description BINDING SITE FOR RESIDUE ACT B 1006 source : AC6 8) chain B residue 659 type sequence Y description BINDING SITE FOR RESIDUE ACT B 1006 source : AC6 9) chain B residue 699 type sequence E description BINDING SITE FOR RESIDUE ACT B 1006 source : AC6 10) chain B residue 733 type sequence D description BINDING SITE FOR RESIDUE ACT B 1006 source : AC6 11) chain B residue 740 type sequence Q description BINDING SITE FOR RESIDUE ACT B 1006 source : AC6 12) chain B residue 753 type sequence K description BINDING SITE FOR RESIDUE ACT B 1006 source : AC6 13) chain B residue 628 type sequence Y description BINDING SITE FOR RESIDUE ACT B 1007 source : AC7 14) chain B residue 642 type sequence R description BINDING SITE FOR RESIDUE ACT B 1007 source : AC7 15) chain B residue 809 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P16930 source Swiss-Prot : SWS_FT_FI7 16) chain B residue 917 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P25093 source Swiss-Prot : SWS_FT_FI8 17) chain B residue 633 type ACT_SITE sequence H description Proton acceptor => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 626 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 699 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 20) chain B residue 701 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 21) chain B residue 628 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 850 type BINDING sequence T description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 23) chain B residue 642 type BINDING sequence R description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 740 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 25) chain B residue 744 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 26) chain B residue 733 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 27) chain B residue 753 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 28) chain B residue 757 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 29) chain B residue 502 type MOD_RES sequence S description N-acetylserine => ECO:0000250|UniProtKB:P16930 source Swiss-Prot : SWS_FT_FI5 30) chain B residue 584 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI6 31) chain B residue 592 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI6 32) chain B residue 753 type catalytic sequence K description 180 source MCSA : MCSA2 33) chain B residue 626 type catalytic sequence D description 180 source MCSA : MCSA2 34) chain B residue 633 type catalytic sequence H description 180 source MCSA : MCSA2 35) chain B residue 699 type catalytic sequence E description 180 source MCSA : MCSA2 36) chain B residue 701 type catalytic sequence E description 180 source MCSA : MCSA2 37) chain B residue 733 type catalytic sequence D description 180 source MCSA : MCSA2 38) chain B residue 737 type catalytic sequence R description 180 source MCSA : MCSA2 39) chain B residue 740 type catalytic sequence Q description 180 source MCSA : MCSA2 40) chain B residue 757 type catalytic sequence T description 180 source MCSA : MCSA2 41) chain B residue 864 type catalytic sequence E description 180 source MCSA : MCSA2

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