6MWQ
Single particle cryoEM structure of a DARPin-aldolase platform in complex with GFP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006096 | biological_process | glycolytic process |
A | 0016829 | molecular_function | lyase activity |
A | 0030335 | biological_process | positive regulation of cell migration |
A | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
A | 0031430 | cellular_component | M band |
A | 0031674 | cellular_component | I band |
A | 0034316 | biological_process | negative regulation of Arp2/3 complex-mediated actin nucleation |
A | 0051289 | biological_process | protein homotetramerization |
B | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006096 | biological_process | glycolytic process |
B | 0016829 | molecular_function | lyase activity |
B | 0030335 | biological_process | positive regulation of cell migration |
B | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
B | 0031430 | cellular_component | M band |
B | 0031674 | cellular_component | I band |
B | 0034316 | biological_process | negative regulation of Arp2/3 complex-mediated actin nucleation |
B | 0051289 | biological_process | protein homotetramerization |
C | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006096 | biological_process | glycolytic process |
C | 0016829 | molecular_function | lyase activity |
C | 0030335 | biological_process | positive regulation of cell migration |
C | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
C | 0031430 | cellular_component | M band |
C | 0031674 | cellular_component | I band |
C | 0034316 | biological_process | negative regulation of Arp2/3 complex-mediated actin nucleation |
C | 0051289 | biological_process | protein homotetramerization |
D | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006096 | biological_process | glycolytic process |
D | 0016829 | molecular_function | lyase activity |
D | 0030335 | biological_process | positive regulation of cell migration |
D | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
D | 0031430 | cellular_component | M band |
D | 0031674 | cellular_component | I band |
D | 0034316 | biological_process | negative regulation of Arp2/3 complex-mediated actin nucleation |
D | 0051289 | biological_process | protein homotetramerization |
G | 0003674 | molecular_function | molecular_function |
G | 0005575 | cellular_component | cellular_component |
G | 0006091 | biological_process | generation of precursor metabolites and energy |
G | 0008218 | biological_process | bioluminescence |
H | 0003674 | molecular_function | molecular_function |
H | 0005575 | cellular_component | cellular_component |
H | 0006091 | biological_process | generation of precursor metabolites and energy |
H | 0008218 | biological_process | bioluminescence |
I | 0003674 | molecular_function | molecular_function |
I | 0005575 | cellular_component | cellular_component |
I | 0006091 | biological_process | generation of precursor metabolites and energy |
I | 0008218 | biological_process | bioluminescence |
J | 0003674 | molecular_function | molecular_function |
J | 0005575 | cellular_component | cellular_component |
J | 0006091 | biological_process | generation of precursor metabolites and energy |
J | 0008218 | biological_process | bioluminescence |
Functional Information from PROSITE/UniProt
site_id | PS00158 |
Number of Residues | 11 |
Details | ALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. IyLEGtLLKPN |
Chain | Residue | Details |
A | ILE390-ASN400 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | MOD_RES: (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132 |
Chain | Residue | Details |
G | GLN65 | |
J | GLN65 | |
I | GLN65 | |
H | GLN65 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | CROSSLNK: 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132 |
Chain | Residue | Details |
G | VAL64 | |
G | CYS66 | |
J | VAL64 | |
J | CYS66 | |
I | VAL64 | |
I | CYS66 | |
H | VAL64 | |
H | CYS66 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD |
Chain | Residue | Details |
A | ARG211 | |
C | SER440 | |
C | SER469 | |
C | ARG472 | |
D | ARG211 | |
D | SER440 | |
D | SER469 | |
D | ARG472 | |
A | SER440 | |
A | SER469 | |
A | ARG472 | |
B | ARG211 | |
B | SER440 | |
B | SER469 | |
B | ARG472 | |
C | ARG211 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | SITE: Essential for substrate cleavage |
Chain | Residue | Details |
A | CYS241 | |
A | LYS276 | |
B | CYS241 | |
B | LYS276 | |
C | CYS241 | |
C | LYS276 | |
D | CYS241 | |
D | LYS276 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Alkylation inactivates the enzyme |
Chain | Residue | Details |
A | LYS315 | |
B | LYS315 | |
C | LYS315 | |
D | LYS315 |
site_id | SWS_FT_FI6 |
Number of Residues | 16 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04075 |
Chain | Residue | Details |
A | SER204 | |
C | SER207 | |
C | SER214 | |
C | SER440 | |
D | SER204 | |
D | SER207 | |
D | SER214 | |
D | SER440 | |
A | SER207 | |
A | SER214 | |
A | SER440 | |
B | SER204 | |
B | SER207 | |
B | SER214 | |
B | SER440 | |
C | SER204 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 |
Chain | Residue | Details |
A | LYS210 | |
B | LYS210 | |
C | LYS210 | |
D | LYS210 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 |
Chain | Residue | Details |
A | LYS267 | |
A | LYS315 | |
B | LYS267 | |
B | LYS315 | |
C | LYS267 | |
C | LYS315 | |
D | LYS267 | |
D | LYS315 |
site_id | SWS_FT_FI9 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P04075 |
Chain | Residue | Details |
A | LYS276 | |
A | LYS498 | |
B | LYS276 | |
B | LYS498 | |
C | LYS276 | |
C | LYS498 | |
D | LYS276 | |
D | LYS498 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | MOD_RES: N6-malonyllysine; alternate => ECO:0000250 |
Chain | Residue | Details |
A | LYS279 | |
B | LYS279 | |
C | LYS279 | |
D | LYS279 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05065 |
Chain | Residue | Details |
A | SER300 | |
B | SER300 | |
C | SER300 | |
D | SER300 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | MOD_RES: N6-malonyllysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS480 | |
B | LYS480 | |
C | LYS480 | |
D | LYS480 |
site_id | SWS_FT_FI13 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P04075 |
Chain | Residue | Details |
A | LYS210 | |
B | LYS210 | |
C | LYS210 | |
D | LYS210 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 222 |
Chain | Residue | Details |
A | ASP202 | electrostatic stabiliser, hydrogen bond acceptor |
A | LYS315 | electrostatic stabiliser, hydrogen bond donor |
A | GLU356 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay |
A | GLU358 | activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction |
A | LYS398 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay |
A | SER469 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 222 |
Chain | Residue | Details |
B | ASP202 | electrostatic stabiliser, hydrogen bond acceptor |
B | LYS315 | electrostatic stabiliser, hydrogen bond donor |
B | GLU356 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay |
B | GLU358 | activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction |
B | LYS398 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay |
B | SER469 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 222 |
Chain | Residue | Details |
C | ASP202 | electrostatic stabiliser, hydrogen bond acceptor |
C | LYS315 | electrostatic stabiliser, hydrogen bond donor |
C | GLU356 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay |
C | GLU358 | activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction |
C | LYS398 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay |
C | SER469 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 222 |
Chain | Residue | Details |
D | ASP202 | electrostatic stabiliser, hydrogen bond acceptor |
D | LYS315 | electrostatic stabiliser, hydrogen bond donor |
D | GLU356 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay |
D | GLU358 | activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction |
D | LYS398 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay |
D | SER469 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |