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

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