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6MWQ

Single particle cryoEM structure of a DARPin-aldolase platform in complex with GFP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006096biological_processglycolytic process
A0016829molecular_functionlyase activity
A0030335biological_processpositive regulation of cell migration
A0030388biological_processfructose 1,6-bisphosphate metabolic process
A0031430cellular_componentM band
A0031674cellular_componentI band
A0034316biological_processnegative regulation of Arp2/3 complex-mediated actin nucleation
A0051289biological_processprotein homotetramerization
B0004332molecular_functionfructose-bisphosphate aldolase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006096biological_processglycolytic process
B0016829molecular_functionlyase activity
B0030335biological_processpositive regulation of cell migration
B0030388biological_processfructose 1,6-bisphosphate metabolic process
B0031430cellular_componentM band
B0031674cellular_componentI band
B0034316biological_processnegative regulation of Arp2/3 complex-mediated actin nucleation
B0051289biological_processprotein homotetramerization
C0004332molecular_functionfructose-bisphosphate aldolase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006096biological_processglycolytic process
C0016829molecular_functionlyase activity
C0030335biological_processpositive regulation of cell migration
C0030388biological_processfructose 1,6-bisphosphate metabolic process
C0031430cellular_componentM band
C0031674cellular_componentI band
C0034316biological_processnegative regulation of Arp2/3 complex-mediated actin nucleation
C0051289biological_processprotein homotetramerization
D0004332molecular_functionfructose-bisphosphate aldolase activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006096biological_processglycolytic process
D0016829molecular_functionlyase activity
D0030335biological_processpositive regulation of cell migration
D0030388biological_processfructose 1,6-bisphosphate metabolic process
D0031430cellular_componentM band
D0031674cellular_componentI band
D0034316biological_processnegative regulation of Arp2/3 complex-mediated actin nucleation
D0051289biological_processprotein homotetramerization
G0003674molecular_functionmolecular_function
G0005575cellular_componentcellular_component
G0006091biological_processgeneration of precursor metabolites and energy
G0008218biological_processbioluminescence
H0003674molecular_functionmolecular_function
H0005575cellular_componentcellular_component
H0006091biological_processgeneration of precursor metabolites and energy
H0008218biological_processbioluminescence
I0003674molecular_functionmolecular_function
I0005575cellular_componentcellular_component
I0006091biological_processgeneration of precursor metabolites and energy
I0008218biological_processbioluminescence
J0003674molecular_functionmolecular_function
J0005575cellular_componentcellular_component
J0006091biological_processgeneration of precursor metabolites and energy
J0008218biological_processbioluminescence
Functional Information from PROSITE/UniProt
site_idPS00158
Number of Residues11
DetailsALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. IyLEGtLLKPN
ChainResidueDetails
AILE390-ASN400

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132
ChainResidueDetails
GGLN65
JGLN65
IGLN65
HGLN65

site_idSWS_FT_FI2
Number of Residues8
DetailsCROSSLNK: 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132
ChainResidueDetails
GVAL64
GCYS66
JVAL64
JCYS66
IVAL64
ICYS66
HVAL64
HCYS66

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD
ChainResidueDetails
AARG211
DARG211
DSER440
DARG472
ASER440
AARG472
BARG211
BSER440
BARG472
CARG211
CSER440
CARG472

site_idSWS_FT_FI4
Number of Residues8
DetailsSITE: Essential for substrate cleavage
ChainResidueDetails
ACYS241
ALYS276
BCYS241
BLYS276
CCYS241
CLYS276
DCYS241
DLYS276

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Alkylation inactivates the enzyme
ChainResidueDetails
ALYS315
BLYS315
CLYS315
DLYS315

site_idSWS_FT_FI6
Number of Residues16
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04075
ChainResidueDetails
ASER204
CSER207
CSER214
CSER440
DSER204
DSER207
DSER214
DSER440
ASER207
ASER214
ASER440
BSER204
BSER207
BSER214
BSER440
CSER204

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075
ChainResidueDetails
ALYS210
BLYS210
CLYS210
DLYS210

site_idSWS_FT_FI8
Number of Residues8
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075
ChainResidueDetails
ALYS267
ALYS315
BLYS267
BLYS315
CLYS267
CLYS315
DLYS267
DLYS315

site_idSWS_FT_FI9
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P04075
ChainResidueDetails
ALYS276
ALYS498
BLYS276
BLYS498
CLYS276
CLYS498
DLYS276
DLYS498

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: N6-malonyllysine; alternate => ECO:0000250
ChainResidueDetails
ALYS279
BLYS279
CLYS279
DLYS279

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05065
ChainResidueDetails
ASER300
BSER300
CSER300
DSER300

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: N6-malonyllysine => ECO:0000250
ChainResidueDetails
ALYS480
BLYS480
CLYS480
DLYS480

site_idSWS_FT_FI13
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P04075
ChainResidueDetails
ALYS210
BLYS210
CLYS210
DLYS210

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 222
ChainResidueDetails
AASP202electrostatic stabiliser, hydrogen bond acceptor
ALYS315electrostatic stabiliser, hydrogen bond donor
AGLU356electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay
AGLU358activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction
ALYS398covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay
ASER469electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

site_idMCSA2
Number of Residues6
DetailsM-CSA 222
ChainResidueDetails
BASP202electrostatic stabiliser, hydrogen bond acceptor
BLYS315electrostatic stabiliser, hydrogen bond donor
BGLU356electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay
BGLU358activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction
BLYS398covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay
BSER469electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

site_idMCSA3
Number of Residues6
DetailsM-CSA 222
ChainResidueDetails
CASP202electrostatic stabiliser, hydrogen bond acceptor
CLYS315electrostatic stabiliser, hydrogen bond donor
CGLU356electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay
CGLU358activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction
CLYS398covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay
CSER469electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

site_idMCSA4
Number of Residues6
DetailsM-CSA 222
ChainResidueDetails
DASP202electrostatic stabiliser, hydrogen bond acceptor
DLYS315electrostatic stabiliser, hydrogen bond donor
DGLU356electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay
DGLU358activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction
DLYS398covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay
DSER469electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

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PDB entries from 2024-04-24

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