eF-site ID 1qqj-AB PDB Code 1qqj Chain A, B 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 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 A residue 126 type sequence D description BINDING SITE FOR RESIDUE CA A 420 source : AC2 6) chain A residue 199 type sequence E description BINDING SITE FOR RESIDUE CA A 420 source : AC2 7) chain A residue 201 type sequence E description BINDING SITE FOR RESIDUE CA A 420 source : AC2 8) chain A residue 233 type sequence D description BINDING SITE FOR RESIDUE CA A 420 source : AC2 9) chain A residue 253 type sequence K description BINDING SITE FOR RESIDUE CA A 420 source : AC2 10) chain A residue 246 type sequence P description BINDING SITE FOR RESIDUE ACT B 2000 source : AC3 11) chain B residue 128 type sequence Y description BINDING SITE FOR RESIDUE ACT B 2000 source : AC3 12) chain B residue 137 type sequence V description BINDING SITE FOR RESIDUE ACT B 2000 source : AC3 13) chain B residue 142 type sequence R description BINDING SITE FOR RESIDUE ACT B 2000 source : AC3 14) chain A residue 128 type sequence Y description BINDING SITE FOR RESIDUE ACT A 2001 source : AC4 15) chain A residue 137 type sequence V description BINDING SITE FOR RESIDUE ACT A 2001 source : AC4 16) chain A residue 142 type sequence R description BINDING SITE FOR RESIDUE ACT A 2001 source : AC4 17) chain B residue 246 type sequence P description BINDING SITE FOR RESIDUE ACT A 2001 source : AC4 18) chain B residue 128 type sequence Y description BINDING SITE FOR RESIDUE CAC B 2003 source : AC5 19) chain B residue 133 type sequence H description BINDING SITE FOR RESIDUE CAC B 2003 source : AC5 20) chain B residue 199 type sequence E description BINDING SITE FOR RESIDUE CAC B 2003 source : AC5 21) chain B residue 237 type sequence R description BINDING SITE FOR RESIDUE CAC B 2003 source : AC5 22) chain B residue 240 type sequence Q description BINDING SITE FOR RESIDUE CAC B 2003 source : AC5 23) chain B residue 253 type sequence K description BINDING SITE FOR RESIDUE CAC B 2003 source : AC5 24) chain A residue 128 type sequence Y description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 25) chain A residue 133 type sequence H description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 26) chain A residue 137 type sequence V description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 27) chain A residue 199 type sequence E description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 28) chain A residue 237 type sequence R description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 29) chain A residue 240 type sequence Q description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 30) chain A residue 253 type sequence K description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 31) chain A residue 350 type sequence T description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 32) chain B residue 247 type sequence L description BINDING SITE FOR RESIDUE CAC A 2004 source : AC6 33) chain A residue 309 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P16930 source Swiss-Prot : SWS_FT_FI7 34) chain B residue 309 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P16930 source Swiss-Prot : SWS_FT_FI7 35) chain B residue 133 type ACT_SITE sequence H description Proton acceptor => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 133 type ACT_SITE sequence H description Proton acceptor => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 126 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 38) chain B residue 199 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 39) chain B residue 201 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 40) chain A residue 126 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 199 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 201 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508789, ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI2 43) chain B residue 350 type BINDING sequence T description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 44) chain B residue 142 type BINDING sequence R description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 45) chain B residue 240 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 46) chain B residue 244 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 47) chain A residue 350 type BINDING sequence T description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 48) chain B residue 128 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 49) chain A residue 128 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 50) chain A residue 142 type BINDING sequence R description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 51) chain A residue 240 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 52) chain A residue 244 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10508789 source Swiss-Prot : SWS_FT_FI3 53) chain B residue 257 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 54) chain A residue 233 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 55) chain A residue 253 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 56) chain A residue 257 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 57) chain B residue 233 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 58) chain B residue 253 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11154690 source Swiss-Prot : SWS_FT_FI4 59) chain B residue 2 type MOD_RES sequence S description N-acetylserine => ECO:0000250|UniProtKB:P16930 source Swiss-Prot : SWS_FT_FI5 60) chain A residue 2 type MOD_RES sequence S description N-acetylserine => ECO:0000250|UniProtKB:P16930 source Swiss-Prot : SWS_FT_FI5 61) chain B residue 84 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI6 62) chain B residue 92 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI6 63) chain A residue 84 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI6 64) chain A residue 92 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21183079 source Swiss-Prot : SWS_FT_FI6 65) chain A residue 253 type catalytic sequence K description 180 source MCSA : MCSA1 66) chain A residue 126 type catalytic sequence D description 180 source MCSA : MCSA1 67) chain A residue 133 type catalytic sequence H description 180 source MCSA : MCSA1 68) chain A residue 199 type catalytic sequence E description 180 source MCSA : MCSA1 69) chain A residue 201 type catalytic sequence E description 180 source MCSA : MCSA1 70) chain A residue 233 type catalytic sequence D description 180 source MCSA : MCSA1 71) chain A residue 237 type catalytic sequence R description 180 source MCSA : MCSA1 72) chain A residue 240 type catalytic sequence Q description 180 source MCSA : MCSA1 73) chain A residue 257 type catalytic sequence T description 180 source MCSA : MCSA1 74) chain A residue 364 type catalytic sequence E description 180 source MCSA : MCSA1 75) chain B residue 253 type catalytic sequence K description 180 source MCSA : MCSA2 76) chain B residue 126 type catalytic sequence D description 180 source MCSA : MCSA2 77) chain B residue 133 type catalytic sequence H description 180 source MCSA : MCSA2 78) chain B residue 199 type catalytic sequence E description 180 source MCSA : MCSA2 79) chain B residue 201 type catalytic sequence E description 180 source MCSA : MCSA2 80) chain B residue 233 type catalytic sequence D description 180 source MCSA : MCSA2 81) chain B residue 237 type catalytic sequence R description 180 source MCSA : MCSA2 82) chain B residue 240 type catalytic sequence Q description 180 source MCSA : MCSA2 83) chain B residue 257 type catalytic sequence T description 180 source MCSA : MCSA2 84) chain B residue 364 type catalytic sequence E description 180 source MCSA : MCSA2

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