Structure of PDB 5tle Chain D

Receptor sequence
>5tleD (length=348) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTEN
TEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSK
GGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCV
LKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKR
CQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAM
ATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFS
YGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPNHAY
3D structure
PDB5tle Bisphosphonate Inhibitors of Mammalian Glycolytic Aldolase.
ChainD
Resolution1.576 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D33 K146 E187 E189 K229 S300 Y363
Catalytic site (residue number reindexed from 1) D33 K146 E187 E189 K229 S300 Y348
Enzyme Commision number 4.1.2.13: fructose-bisphosphate aldolase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 RD1 D A31 D33 S35 S38 K107 K229 L270 G272 G302 R303 A31 D33 S35 S38 K107 K229 L270 G272 G302 R303
Gene Ontology
Molecular Function
GO:0004332 fructose-bisphosphate aldolase activity
GO:0005515 protein binding
GO:0016829 lyase activity
Biological Process
GO:0006096 glycolytic process
GO:0030335 positive regulation of cell migration
GO:0030388 fructose 1,6-bisphosphate metabolic process
GO:0034316 negative regulation of Arp2/3 complex-mediated actin nucleation
GO:0051289 protein homotetramerization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0031430 M band
GO:0031674 I band

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5tle, PDBe:5tle, PDBj:5tle
PDBsum5tle
PubMed30418024
UniProtP00883|ALDOA_RABIT Fructose-bisphosphate aldolase A (Gene Name=ALDOA)

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