eF-site ID 4mb8-D PDB Code 4mb8 Chain D click to enlarge Title Evolutionary history and metabolic insights of ancient mammalian uricases Classification OXIDOREDUCTASE Compound Uricase Source (4MB8) Sequence D:  VEFVRTGYGKDMVKVLHIQRDGKYHSIKEVATSVQLTLSS KKDYLHGDNSDIIPTDTIKNTVHVLAKFKGIKSIEAFAMN ICEHFLSSFNHVIRAQVYVEEVPWKRFEKNGVKHVHAFIH TPTGTHFCEVEQMKSGPPVIHSGIKDLKVLKTTQSGFEGF IKDQFTTLPEVKDRCFATQVYCKWRYHQGRDVDFEATWDT VRDIVLKKFAGPYDKGEYSPSVQKTLYDIQVLSLSRVPEI EDMEISLPNIHYFNIDMSKMGLINKEEVLLPLDNPYGKIT GTVKRKLSSR Description Functional site 1) chain D residue 170 type sequence F description BINDING SITE FOR RESIDUE ACT D 401 source : AC2 2) chain D residue 187 type sequence R description BINDING SITE FOR RESIDUE ACT D 401 source : AC2 3) chain D residue 291 type sequence K description BINDING SITE FOR RESIDUE ACT D 402 source : AC3 4) chain D residue 23 type ACT_SITE sequence K description Charge relay system => ECO:0000250|UniProtKB:D0VWQ1 source Swiss-Prot : SWS_FT_FI1 5) chain D residue 68 type ACT_SITE sequence T description Charge relay system => ECO:0000250|UniProtKB:D0VWQ1 source Swiss-Prot : SWS_FT_FI1 6) chain D residue 264 type ACT_SITE sequence H description Charge relay system => ECO:0000250|UniProtKB:D0VWQ1 source Swiss-Prot : SWS_FT_FI1 7) chain D residue 68 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI2 8) chain D residue 69 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI2 9) chain D residue 170 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI2 10) chain D residue 187 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI2 11) chain D residue 235 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI2 12) chain D residue 236 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI2 13) chain D residue 262 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q00511 source Swiss-Prot : SWS_FT_FI2 14) chain D residue 23 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P25688 source Swiss-Prot : SWS_FT_FI4 15) chain D residue 221 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P25688 source Swiss-Prot : SWS_FT_FI4 16) chain D residue 228 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P25688 source Swiss-Prot : SWS_FT_FI4 17) chain D residue 27 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25688 source Swiss-Prot : SWS_FT_FI5 18) chain D residue 36 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25688 source Swiss-Prot : SWS_FT_FI5 19) chain D residue 118 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25688 source Swiss-Prot : SWS_FT_FI5 20) chain D residue 122 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25688 source Swiss-Prot : SWS_FT_FI5 21) chain D residue 164 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25688 source Swiss-Prot : SWS_FT_FI5 22) chain D residue 175 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25688 source Swiss-Prot : SWS_FT_FI5 23) chain D residue 185 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25688 source Swiss-Prot : SWS_FT_FI5 24) chain D residue 278 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25688 source Swiss-Prot : SWS_FT_FI5 25) chain D residue 39 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P25688 source Swiss-Prot : SWS_FT_FI6 26) chain D residue 63 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P25688 source Swiss-Prot : SWS_FT_FI6 27) chain D residue 232 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P25688 source Swiss-Prot : SWS_FT_FI6 28) chain D residue 289 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P25688 source Swiss-Prot : SWS_FT_FI7

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