eF-site ID 6mwq-ABCDGHIJ PDB Code 6mwq Chain A, B, C, D, G, H, I, J 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 A:  SGSDLGKKLLEAARAGQDDEVRILMANGADVNALDRFGLT PLHLAAQRGHLEIVEVLLKCGADVNAADLWGQTPLHLAAT AGHLEIVEVLLKYGADVNALDLIGKTPLHLTAIDGHLEIV EVLLKHGADVNAQDKFGKTAFDISIDNGNEDLAEILQKLN LSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEEN RRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFP QVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERC AQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYA SICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYK ALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVT ALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKP WALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALAN SLACQGKYTPSGQ B:  SGSDLGKKLLEAARAGQDDEVRILMANGADVNALDRFGLT PLHLAAQRGHLEIVEVLLKCGADVNAADLWGQTPLHLAAT AGHLEIVEVLLKYGADVNALDLIGKTPLHLTAIDGHLEIV EVLLKHGADVNAQDKFGKTAFDISIDNGNEDLAEILQKLN LSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEEN RRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFP QVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERC AQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYA SICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYK ALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVT ALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKP WALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALAN SLACQGKYTPSGQ C:  SGSDLGKKLLEAARAGQDDEVRILMANGADVNALDRFGLT PLHLAAQRGHLEIVEVLLKCGADVNAADLWGQTPLHLAAT AGHLEIVEVLLKYGADVNALDLIGKTPLHLTAIDGHLEIV EVLLKHGADVNAQDKFGKTAFDISIDNGNEDLAEILQKLN LSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEEN RRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFP QVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERC AQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYA SICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYK ALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVT ALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKP WALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALAN SLACQGKYTPSGQ D:  SGSDLGKKLLEAARAGQDDEVRILMANGADVNALDRFGLT PLHLAAQRGHLEIVEVLLKCGADVNAADLWGQTPLHLAAT AGHLEIVEVLLKYGADVNALDLIGKTPLHLTAIDGHLEIV EVLLKHGADVNAQDKFGKTAFDISIDNGNEDLAEILQKLN LSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEEN RRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFP QVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERC AQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYA SICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYK ALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVT ALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKP WALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALAN SLACQGKYTPSGQ G:  SKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGK LTLKFICTTGKLPVPWPTLVTTLVQCFSRYPDHMKQHDFF KSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIE LKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVN FKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQ SALSKDPNEKRDHMVLLEFVTAAGIT H:  SKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGK LTLKFICTTGKLPVPWPTLVTTVQCFSRYPDHMKQHDFFK SAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIEL KGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNF KIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQS ALSKDPNEKRDHMVLLEFVTAAGIT I:  SKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGK LTLKFICTTGKLPVPWPTLVTTVQCFSRYPDHMKQHDFFK SAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIEL KGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNF KIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQS ALSKDPNEKRDHMVLLEFVTAAGIT J:  SKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGK LTLKFICTTGKLPVPWPTLVTTVQCFSRYPDHMKQHDFFK SAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIEL KGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNF KIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQS ALSKDPNEKRDHMVLLEFVTAAGIT Description Functional site 1) chain A residue 202 type catalytic sequence D description 222 source MCSA : MCSA1 2) chain A residue 315 type catalytic sequence K description 222 source MCSA : MCSA1 3) chain A residue 356 type catalytic sequence E description 222 source MCSA : MCSA1 4) chain A residue 358 type catalytic sequence E description 222 source MCSA : MCSA1 5) chain A residue 398 type catalytic sequence K description 222 source MCSA : MCSA1 6) chain A residue 469 type catalytic sequence S description 222 source MCSA : MCSA1 7) chain B residue 202 type catalytic sequence D description 222 source MCSA : MCSA2 8) chain B residue 315 type catalytic sequence K description 222 source MCSA : MCSA2 9) chain B residue 356 type catalytic sequence E description 222 source MCSA : MCSA2 10) chain B residue 358 type catalytic sequence E description 222 source MCSA : MCSA2 11) chain B residue 398 type catalytic sequence K description 222 source MCSA : MCSA2 12) chain B residue 469 type catalytic sequence S description 222 source MCSA : MCSA2 13) chain C residue 202 type catalytic sequence D description 222 source MCSA : MCSA3 14) chain C residue 315 type catalytic sequence K description 222 source MCSA : MCSA3 15) chain C residue 356 type catalytic sequence E description 222 source MCSA : MCSA3 16) chain C residue 358 type catalytic sequence E description 222 source MCSA : MCSA3 17) chain C residue 398 type catalytic sequence K description 222 source MCSA : MCSA3 18) chain C residue 469 type catalytic sequence S description 222 source MCSA : MCSA3 19) chain D residue 202 type catalytic sequence D description 222 source MCSA : MCSA4 20) chain D residue 315 type catalytic sequence K description 222 source MCSA : MCSA4 21) chain D residue 356 type catalytic sequence E description 222 source MCSA : MCSA4 22) chain D residue 358 type catalytic sequence E description 222 source MCSA : MCSA4 23) chain D residue 398 type catalytic sequence K description 222 source MCSA : MCSA4 24) chain D residue 469 type catalytic sequence S description 222 source MCSA : MCSA4 25) chain A residue 267 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 26) chain A residue 315 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 27) chain B residue 267 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 28) chain B residue 315 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 29) chain C residue 267 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 30) chain C residue 315 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 31) chain D residue 267 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 32) chain D residue 315 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI8 33) chain A residue 300 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P05065 source Swiss-Prot : SWS_FT_FI11 34) chain B residue 300 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P05065 source Swiss-Prot : SWS_FT_FI11 35) chain C residue 300 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P05065 source Swiss-Prot : SWS_FT_FI11 36) chain D residue 300 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P05065 source Swiss-Prot : SWS_FT_FI11 37) chain A residue 480 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 38) chain B residue 480 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 39) chain C residue 480 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 40) chain D residue 480 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 41) chain G residue 65 type MOD_RES sequence Q description (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132 source Swiss-Prot : SWS_FT_FI1 42) chain J residue 65 type MOD_RES sequence Q description (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132 source Swiss-Prot : SWS_FT_FI1 43) chain I residue 65 type MOD_RES sequence Q description (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132 source Swiss-Prot : SWS_FT_FI1 44) chain H residue 65 type MOD_RES sequence Q description (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132 source Swiss-Prot : SWS_FT_FI1 45) chain A residue 279 type MOD_RES sequence K description N6-malonyllysine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI10 46) chain B residue 279 type MOD_RES sequence K description N6-malonyllysine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI10 47) chain C residue 279 type MOD_RES sequence K description N6-malonyllysine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI10 48) chain D residue 279 type MOD_RES sequence K description N6-malonyllysine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI10 49) chain G residue 64 type CROSSLNK sequence V description 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132 source Swiss-Prot : SWS_FT_FI2 50) chain G residue 66 type CROSSLNK sequence C description 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132 source Swiss-Prot : SWS_FT_FI2 51) chain J residue 64 type CROSSLNK sequence V description 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132 source Swiss-Prot : SWS_FT_FI2 52) chain J residue 66 type CROSSLNK sequence C description 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132 source Swiss-Prot : SWS_FT_FI2 53) chain I residue 64 type CROSSLNK sequence V description 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132 source Swiss-Prot : SWS_FT_FI2 54) chain I residue 66 type CROSSLNK sequence C description 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132 source Swiss-Prot : SWS_FT_FI2 55) chain H residue 64 type CROSSLNK sequence V description 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132 source Swiss-Prot : SWS_FT_FI2 56) chain H residue 66 type CROSSLNK sequence C description 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132 source Swiss-Prot : SWS_FT_FI2 57) chain A residue 204 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 58) chain C residue 207 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 59) chain C residue 214 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 60) chain C residue 440 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 61) chain D residue 204 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 62) chain D residue 207 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 63) chain D residue 214 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 64) chain D residue 440 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 65) chain A residue 207 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 66) chain A residue 214 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 67) chain A residue 440 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 68) chain B residue 204 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 69) chain B residue 207 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 70) chain B residue 214 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 71) chain B residue 440 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 72) chain C residue 204 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI6 73) chain A residue 210 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI7 74) chain B residue 210 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI7 75) chain C residue 210 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI7 76) chain D residue 210 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI7 77) chain A residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9 78) chain A residue 498 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9 79) chain B residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9 80) chain B residue 498 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9 81) chain C residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9 82) chain C residue 498 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9 83) chain D residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9 84) chain D residue 498 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P04075 source Swiss-Prot : SWS_FT_FI9 85) chain A residue 211 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 86) chain D residue 211 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 87) chain D residue 440 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 88) chain D residue 472 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 89) chain A residue 440 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 90) chain A residue 472 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 91) chain B residue 211 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 92) chain B residue 440 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 93) chain B residue 472 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 94) chain C residue 211 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 95) chain C residue 440 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 96) chain C residue 472 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD source Swiss-Prot : SWS_FT_FI3 97) chain A residue 241 type SITE sequence C description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 98) chain A residue 276 type SITE sequence K description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 99) chain B residue 241 type SITE sequence C description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 100) chain B residue 276 type SITE sequence K description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 101) chain C residue 241 type SITE sequence C description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 102) chain C residue 276 type SITE sequence K description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 103) chain D residue 241 type SITE sequence C description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 104) chain D residue 276 type SITE sequence K description Essential for substrate cleavage source Swiss-Prot : SWS_FT_FI4 105) chain A residue 315 type SITE sequence K description Alkylation inactivates the enzyme source Swiss-Prot : SWS_FT_FI5 106) chain B residue 315 type SITE sequence K description Alkylation inactivates the enzyme source Swiss-Prot : SWS_FT_FI5 107) chain C residue 315 type SITE sequence K description Alkylation inactivates the enzyme source Swiss-Prot : SWS_FT_FI5 108) chain D residue 315 type SITE sequence K description Alkylation inactivates the enzyme source Swiss-Prot : SWS_FT_FI5 109) chain A residue 390-400 type prosite sequence IYLEGTLLKPN description ALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. IyLEGtLLKPN source prosite : PS00158 110) chain A 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 111) 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 112) chain C 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 113) chain D 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

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