eF-site ID 6mwq-A
PDB Code 6mwq
Chain A

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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
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 A
residue 267
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075
source Swiss-Prot : SWS_FT_FI8

8) chain A
residue 315
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075
source Swiss-Prot : SWS_FT_FI8

9) chain A
residue 300
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P05065
source Swiss-Prot : SWS_FT_FI11

10) chain A
residue 480
type MOD_RES
sequence K
description N6-malonyllysine => ECO:0000250
source Swiss-Prot : SWS_FT_FI12

11) chain A
residue 279
type MOD_RES
sequence K
description N6-malonyllysine; alternate => ECO:0000250
source Swiss-Prot : SWS_FT_FI10

12) chain A
residue 204
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P04075
source Swiss-Prot : SWS_FT_FI6

13) chain A
residue 207
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P04075
source Swiss-Prot : SWS_FT_FI6

14) chain A
residue 214
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P04075
source Swiss-Prot : SWS_FT_FI6

15) chain A
residue 440
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P04075
source Swiss-Prot : SWS_FT_FI6

16) chain A
residue 210
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075
source Swiss-Prot : SWS_FT_FI7

17) chain A
residue 276
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P04075
source Swiss-Prot : SWS_FT_FI9

18) chain A
residue 498
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P04075
source Swiss-Prot : SWS_FT_FI9

19) chain A
residue 211
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD
source Swiss-Prot : SWS_FT_FI3

20) chain A
residue 440
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD
source Swiss-Prot : SWS_FT_FI3

21) chain A
residue 472
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD
source Swiss-Prot : SWS_FT_FI3

22) chain A
residue 241
type SITE
sequence C
description Essential for substrate cleavage
source Swiss-Prot : SWS_FT_FI4

23) chain A
residue 276
type SITE
sequence K
description Essential for substrate cleavage
source Swiss-Prot : SWS_FT_FI4

24) chain A
residue 315
type SITE
sequence K
description Alkylation inactivates the enzyme
source Swiss-Prot : SWS_FT_FI5

25) chain A
residue 390-400
type prosite
sequence IYLEGTLLKPN
description ALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. IyLEGtLLKPN
source prosite : PS00158

26) 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


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