eF-site ID 1qco-B PDB Code 1qco Chain B click to enlarge Title CRYSTAL STRUCTURE OF FUMARYLACETOACETATE HYDROLASE COMPLEXED WITH FUMARATE AND ACETOACETATE Classification HYDROLASE Compound FUMARYLACETOACETATE HYDROLASE Source Mus musculus (Mouse) (FAAA_MOUSE) Sequence B:  GSMSFIPVAEDSDFPIQNLPYGVFSTQSNPKPRIGVAIGD QILDLSVIKHLFTGPALSKHQHVFDETTLNNFMGLGQAAW KEARASLQNLLSASQARLRDDKELRQRAFTSQASATMHLP ATIGDYTDFYSSRQHATNVGIMFRGKENALLPNWLHLPVG YHGRASSIVVSGTPIRRPMGQMRPDNSKPPVYGACRLLDM ELEMAFFVGPGNRFGEPIPISKAHEHIFGMVLMNDWSARD IQQWEYVPLGPFLGKSFGTTISPWVVPMDALMPFVVPNPK QDPKPLPYLCHSQPYTFDINLSVSLKGEGMSQAATICRSN FKHMYWTMLQQLTHHSVNGCNLRPGDLLASGTISGSDPES FGSMLELSWKGTKAIDVGQGQTRTFLLDGDEVIITGHCQG DGYRVGFGQCAGKVLPALS Description Functional site 1) chain B residue 626 type sequence D description BINDING SITE FOR RESIDUE CA B 1001 source : AC1 2) chain B residue 699 type sequence E description BINDING SITE FOR RESIDUE CA B 1001 source : AC1 3) chain B residue 701 type sequence E description BINDING SITE FOR RESIDUE CA B 1001 source : AC1 4) chain B residue 733 type sequence D description BINDING SITE FOR RESIDUE CA B 1001 source : AC1 5) chain B residue 654 type sequence H description BINDING SITE FOR RESIDUE NI B 1003 source : AC3 6) chain B residue 511 type sequence D description BINDING SITE FOR RESIDUE NI B 1004 source : AC4 7) chain B residue 895 type sequence H description BINDING SITE FOR RESIDUE NI B 1004 source : AC4 8) chain B residue 722 type sequence H description BINDING SITE FOR RESIDUE NI B 1005 source : AC5 9) chain B residue 499 type sequence G description BINDING SITE FOR RESIDUE NI B 1007 source : AC7 10) chain B residue 746 type sequence P description BINDING SITE FOR RESIDUE FUM A 1008 source : AC8 11) chain B residue 628 type sequence Y description BINDING SITE FOR RESIDUE FUM B 1009 source : AC9 12) chain B residue 637 type sequence V description BINDING SITE FOR RESIDUE FUM B 1009 source : AC9 13) chain B residue 642 type sequence R description BINDING SITE FOR RESIDUE FUM B 1009 source : AC9 14) chain B residue 740 type sequence Q description BINDING SITE FOR RESIDUE FUM B 1009 source : AC9 15) chain B residue 744 type sequence Y description BINDING SITE FOR RESIDUE FUM B 1009 source : AC9 16) chain B residue 626 type sequence D description BINDING SITE FOR RESIDUE AAE B 1011 source : BC2 17) chain B residue 627 type sequence F description BINDING SITE FOR RESIDUE AAE B 1011 source : BC2 18) chain B residue 628 type sequence Y description BINDING SITE FOR RESIDUE AAE B 1011 source : BC2 19) chain B residue 633 type sequence H description BINDING SITE FOR RESIDUE AAE B 1011 source : BC2 20) chain B residue 659 type sequence Y description BINDING SITE FOR RESIDUE AAE B 1011 source : BC2 21) chain B residue 699 type sequence E description BINDING SITE FOR RESIDUE AAE B 1011 source : BC2 22) chain B residue 701 type sequence E description BINDING SITE FOR RESIDUE AAE B 1011 source : BC2 23) chain B residue 733 type sequence D description BINDING SITE FOR RESIDUE AAE B 1011 source : BC2 24) chain B residue 753 type sequence K description BINDING SITE FOR RESIDUE AAE B 1011 source : BC2 25) chain B residue 849 type sequence G description BINDING SITE FOR RESIDUE AAE B 1011 source : BC2 26) chain B residue 850 type sequence T description BINDING SITE FOR RESIDUE AAE B 1011 source : BC2 27) chain B residue 626 type catalytic sequence D description 180 source MCSA : MCSA2 28) chain B residue 864 type catalytic sequence E description 180 source MCSA : MCSA2 29) chain B residue 633 type catalytic sequence H description 180 source MCSA : MCSA2 30) chain B residue 699 type catalytic sequence E description 180 source MCSA : MCSA2 31) chain B residue 701 type catalytic sequence E description 180 source MCSA : MCSA2 32) chain B residue 733 type catalytic sequence D description 180 source MCSA : MCSA2 33) chain B residue 737 type catalytic sequence R description 180 source MCSA : MCSA2 34) chain B residue 740 type catalytic sequence Q description 180 source MCSA : MCSA2 35) chain B residue 753 type catalytic sequence K description 180 source MCSA : MCSA2 36) chain B residue 757 type catalytic sequence T description 180 source MCSA : MCSA2 37) chain B residue 633 type ACT_SITE sequence H description Proton acceptor => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 626 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 39) chain B residue 699 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 40) chain B residue 701 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 41) chain B residue 850 type BINDING sequence T description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 42) chain B residue 628 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 43) chain B residue 642 type BINDING sequence R description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 44) chain B residue 740 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 45) chain B residue 744 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 46) chain B residue 733 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 47) chain B residue 753 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 48) chain B residue 757 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 49) chain B residue 502 type MOD_RES sequence S description N-acetylserine => ECO:0000250|UniProtKB:P16930 source Swiss-Prot : SWS_FT_FI5 50) chain B residue 584 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI6 51) chain B residue 592 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI6 52) chain B residue 809 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P16930 source Swiss-Prot : SWS_FT_FI7 53) chain B residue 917 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P25093 source Swiss-Prot : SWS_FT_FI8

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