eF-site ID 6mwq-B PDB Code 6mwq Chain B click to enlarge Title Single particle cryoEM structure of a DARPin-aldolase platform in complex with GFP Classification LYASE/FLUORESCENT PROTEIN Compound DARPin, Muscle-type aldolase chimeric fusion Source (GFP_AEQVI) Sequence B:  SGSDLGKKLLEAARAGQDDEVRILMANGADVNALDRFGLT PLHLAAQRGHLEIVEVLLKCGADVNAADLWGQTPLHLAAT AGHLEIVEVLLKYGADVNALDLIGKTPLHLTAIDGHLEIV EVLLKHGADVNAQDKFGKTAFDISIDNGNEDLAEILQKLN LSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEEN RRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFP QVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERC AQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYA SICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYK ALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVT ALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKP WALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALAN SLACQGKYTPSGQ Description Functional site 1) chain B residue 202 type catalytic sequence D description 222 source MCSA : MCSA2 2) chain B residue 315 type catalytic sequence K description 222 source MCSA : MCSA2 3) chain B residue 356 type catalytic sequence E description 222 source MCSA : MCSA2 4) chain B residue 358 type catalytic sequence E description 222 source MCSA : MCSA2 5) chain B residue 398 type catalytic sequence K description 222 source MCSA : MCSA2 6) chain B residue 469 type catalytic sequence S description 222 source MCSA : MCSA2 7) chain B residue 279 type MOD_RES sequence K description N6-malonyllysine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI10 8) chain B residue 300 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P05065 source Swiss-Prot : SWS_FT_FI11 9) chain B residue 480 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 10) chain B residue 210 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI13 11) chain B residue 211 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 12) chain B residue 440 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 13) chain B residue 469 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 14) chain B residue 472 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 15) chain B residue 241 type SITE sequence C description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 16) chain B residue 276 type SITE sequence K description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 17) chain B residue 315 type SITE sequence K description Alkylation inactivates the enzyme source Swiss-Prot : SWS_FT_FI5 18) chain B residue 204 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 19) chain B residue 207 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 20) chain B residue 214 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 21) chain B residue 440 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 22) chain B residue 210 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI7 23) chain B residue 267 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 24) chain B residue 315 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 25) chain B residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9 26) chain B residue 498 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9

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