eF-site ID 1qqj-B PDB Code 1qqj Chain B click to enlarge Title CRYSTAL STRUCTURE OF MOUSE FUMARYLACETOACETATE HYDROLASE REFINED AT 1.55 ANGSTROM RESOLUTION Classification HYDROLASE Compound FUMARYLACETOACETATE HYDROLASE Source Mus musculus (Mouse) (FAAA_MOUSE) Sequence B:  MSFIPVAEDSDFPIQNLPYGVFSTQSNPKPRIGVAIGDQI LDLSVIKHLFTGPALSKHQHVFDETTLNNFMGLGQAAWKE ARASLQNLLSASQARLRDDKELRQRAFTSQASATMHLPAT IGDYTDFYSSRQHATNVGIMFRGKENALLPNWLHLPVGYH GRASSIVVSGTPIRRPMGQMRPDNSKPPVYGACRLLDMEL EMAFFVGPGNRFGEPIPISKAHEHIFGMVLMNDWSARDIQ QWEYVPLGPFLGKSFGTTISPWVVPMDALMPFVVPNPKQD PKPLPYLCHSQPYTFDINLSVSLKGEGMSQAATICRSNFK HMYWTMLQQLTHHSVNGCNLRPGDLLASGTISGSDPESFG SMLELSWKGTKAIDVGQGQTRTFLLDGDEVIITGHCQGDG YRVGFGQCAGKVLPAL Description Functional site 1) chain B residue 126 type sequence D description BINDING SITE FOR RESIDUE CA B 420 source : AC1 2) chain B residue 199 type sequence E description BINDING SITE FOR RESIDUE CA B 420 source : AC1 3) chain B residue 201 type sequence E description BINDING SITE FOR RESIDUE CA B 420 source : AC1 4) chain B residue 233 type sequence D description BINDING SITE FOR RESIDUE CA B 420 source : AC1 5) chain B residue 128 type sequence Y description BINDING SITE FOR RESIDUE ACT B 2000 source : AC3 6) chain B residue 137 type sequence V description BINDING SITE FOR RESIDUE ACT B 2000 source : AC3 7) chain B residue 142 type sequence R description BINDING SITE FOR RESIDUE ACT B 2000 source : AC3 8) chain B residue 246 type sequence P description BINDING SITE FOR RESIDUE ACT A 2001 source : AC4 9) chain B residue 128 type sequence Y description BINDING SITE FOR RESIDUE CAC B 2003 source : AC5 10) chain B residue 133 type sequence H description BINDING SITE FOR RESIDUE CAC B 2003 source : AC5 11) chain B residue 199 type sequence E description BINDING SITE FOR RESIDUE CAC B 2003 source : AC5 12) chain B residue 237 type sequence R description BINDING SITE FOR RESIDUE CAC B 2003 source : AC5 13) chain B residue 240 type sequence Q description BINDING SITE FOR RESIDUE CAC B 2003 source : AC5 14) chain B residue 253 type sequence K description BINDING SITE FOR RESIDUE CAC B 2003 source : AC5 15) chain B residue 247 type sequence L description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 16) chain B residue 126 type catalytic sequence D description 180 source MCSA : MCSA2 17) chain B residue 364 type catalytic sequence E description 180 source MCSA : MCSA2 18) chain B residue 133 type catalytic sequence H description 180 source MCSA : MCSA2 19) chain B residue 199 type catalytic sequence E description 180 source MCSA : MCSA2 20) chain B residue 201 type catalytic sequence E description 180 source MCSA : MCSA2 21) chain B residue 233 type catalytic sequence D description 180 source MCSA : MCSA2 22) chain B residue 237 type catalytic sequence R description 180 source MCSA : MCSA2 23) chain B residue 240 type catalytic sequence Q description 180 source MCSA : MCSA2 24) chain B residue 253 type catalytic sequence K description 180 source MCSA : MCSA2 25) chain B residue 257 type catalytic sequence T description 180 source MCSA : MCSA2 26) chain B residue 126 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 27) chain B residue 199 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 28) chain B residue 201 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 29) chain B residue 350 type BINDING sequence T description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 30) chain B residue 128 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 31) chain B residue 142 type BINDING sequence R description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 32) chain B residue 240 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 33) chain B residue 244 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 34) chain B residue 233 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 35) chain B residue 253 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 36) chain B residue 257 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 37) chain B residue 133 type ACT_SITE sequence H description Proton acceptor => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 2 type MOD_RES sequence S description N-acetylserine => ECO:0000250|UniProtKB:P16930 source Swiss-Prot : SWS_FT_FI5 39) chain B residue 309 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P16930 source Swiss-Prot : SWS_FT_FI7 40) chain B residue 84 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI6 41) chain B residue 92 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI6

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