eF-site ID 1qqj-A PDB Code 1qqj Chain A click to enlarge Title CRYSTAL STRUCTURE OF MOUSE FUMARYLACETOACETATE HYDROLASE REFINED AT 1.55 ANGSTROM RESOLUTION Classification HYDROLASE Compound FUMARYLACETOACETATE HYDROLASE Source null (FAAA_MOUSE) Sequence A:  MSFIPVAEDSDFPIQNLPYGVFSTQSNPKPRIGVAIGDQI LDLSVIKHLFTGPALSKHQHVFDETTLNNFMGLGQAAWKE ARASLQNLLSASQARLRDDKELRQRAFTSQASATMHLPAT IGDYTDFYSSRQHATNVGIMFRGKENALLPNWLHLPVGYH GRASSIVVSGTPIRRPMGQMRPDNSKPPVYGACRLLDMEL EMAFFVGPGNRFGEPIPISKAHEHIFGMVLMNDWSARDIQ QWEYVPLGPFLGKSFGTTISPWVVPMDALMPFVVPNPKQD PKPLPYLCHSQPYTFDINLSVSLKGEGMSQAATICRSNFK HMYWTMLQQLTHHSVNGCNLRPGDLLASGTISGSDPESFG SMLELSWKGTKAIDVGQGQTRTFLLDGDEVIITGHCQGDG YRVGFGQCAGKVLPAL Description Functional site 1) chain A residue 126 type sequence D description BINDING SITE FOR RESIDUE CA A 420 source : AC2 2) chain A residue 199 type sequence E description BINDING SITE FOR RESIDUE CA A 420 source : AC2 3) chain A residue 201 type sequence E description BINDING SITE FOR RESIDUE CA A 420 source : AC2 4) chain A residue 233 type sequence D description BINDING SITE FOR RESIDUE CA A 420 source : AC2 5) chain A residue 253 type sequence K description BINDING SITE FOR RESIDUE CA A 420 source : AC2 6) chain A residue 246 type sequence P description BINDING SITE FOR RESIDUE ACT B 2000 source : AC3 7) chain A residue 128 type sequence Y description BINDING SITE FOR RESIDUE ACT A 2001 source : AC4 8) chain A residue 137 type sequence V description BINDING SITE FOR RESIDUE ACT A 2001 source : AC4 9) chain A residue 142 type sequence R description BINDING SITE FOR RESIDUE ACT A 2001 source : AC4 10) chain A residue 128 type sequence Y description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 11) chain A residue 133 type sequence H description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 12) chain A residue 137 type sequence V description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 13) chain A residue 199 type sequence E description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 14) chain A residue 237 type sequence R description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 15) chain A residue 240 type sequence Q description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 16) chain A residue 253 type sequence K description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 17) chain A residue 350 type sequence T description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 18) chain A residue 309 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P16930 source Swiss-Prot : SWS_FT_FI7 19) chain A residue 133 type ACT_SITE sequence H description Proton acceptor => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 126 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 199 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 201 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 350 type BINDING sequence T description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 128 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 142 type BINDING sequence R description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 240 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 244 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 233 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 29) chain A residue 253 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 30) chain A residue 257 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 31) chain A residue 2 type MOD_RES sequence S description N-acetylserine => ECO:0000250|UniProtKB:P16930 source Swiss-Prot : SWS_FT_FI5 32) chain A residue 84 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI6 33) chain A residue 92 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI6 34) chain A residue 253 type catalytic sequence K description 180 source MCSA : MCSA1 35) chain A residue 126 type catalytic sequence D description 180 source MCSA : MCSA1 36) chain A residue 133 type catalytic sequence H description 180 source MCSA : MCSA1 37) chain A residue 199 type catalytic sequence E description 180 source MCSA : MCSA1 38) chain A residue 201 type catalytic sequence E description 180 source MCSA : MCSA1 39) chain A residue 233 type catalytic sequence D description 180 source MCSA : MCSA1 40) chain A residue 237 type catalytic sequence R description 180 source MCSA : MCSA1 41) chain A residue 240 type catalytic sequence Q description 180 source MCSA : MCSA1 42) chain A residue 257 type catalytic sequence T description 180 source MCSA : MCSA1 43) chain A residue 364 type catalytic sequence E description 180 source MCSA : MCSA1

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