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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

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
A0006096biological_processglycolytic process
A0016829molecular_functionlyase activity
A0030335biological_processpositive regulation of cell migration
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
B0006096biological_processglycolytic process
B0016829molecular_functionlyase activity
B0030335biological_processpositive regulation of cell migration
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
C0006096biological_processglycolytic process
C0016829molecular_functionlyase activity
C0030335biological_processpositive regulation of cell migration
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
D0006096biological_processglycolytic process
D0016829molecular_functionlyase activity
D0030335biological_processpositive regulation of cell migration
D0031430cellular_componentM band
D0031674cellular_componentI band
D0034316biological_processnegative regulation of Arp2/3 complex-mediated actin nucleation
D0051289biological_processprotein homotetramerization
G0006091biological_processgeneration of precursor metabolites and energy
G0008218biological_processbioluminescence
H0006091biological_processgeneration of precursor metabolites and energy
H0008218biological_processbioluminescence
I0006091biological_processgeneration of precursor metabolites and energy
I0008218biological_processbioluminescence
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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11779856","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Schiff-base intermediate with dihydroxyacetone-P","evidences":[{"source":"PubMed","id":"11779856","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10504235","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6ALD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues8
DetailsSite: {"description":"Essential for substrate cleavage"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Alkylation inactivates the enzyme"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues16
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues8
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"N6-malonyllysine; alternate","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P05065","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
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
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_idMCSA3
Number of Residues6
DetailsM-CSA 222
ChainResidueDetails
site_idMCSA4
Number of Residues6
DetailsM-CSA 222
ChainResidueDetails
GGLN179electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2025-07-09

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