Structure of PDB 1dos Chain A

Receptor sequence
>1dosA (length=358) Species: 562 (Escherichia coli) [Search protein sequence]
SKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTDSINAVLETAA
KVKAPVIVQFSNGGASFIAGKGVKSDVPQGAAILGAISGAHHVHQMAEHY
GVPVILHTDHCAKKLLPWIDGLLDAGEKHFAATGKPLFSSHMIDLSEESL
QENIEICSKYLERMSKIGMTLEIELGCTGGEEDGVDNSHMDASALYTQPE
DVDYAYTELSKISPRFTIAASFGNVHGVYKAGNVVLTPTILRDSQEYVSK
KHNLPHNSLNFVFHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVL
NYYKANEAYLQGQLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARLEKAFQ
ELNAIDVL
3D structure
PDB1dos Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase.
ChainA
Resolution1.67 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D109 H110 E182 H226 H264 N286
Catalytic site (residue number reindexed from 1) D109 H110 E182 H226 H264 N286
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 ZN A H110 E174 H226 H264 H110 E174 H226 H264
Gene Ontology
Molecular Function
GO:0004332 fructose-bisphosphate aldolase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0016832 aldehyde-lyase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1dos, PDBe:1dos, PDBj:1dos
PDBsum1dos
PubMed8836102
UniProtP0AB71|ALF_ECOLI Fructose-bisphosphate aldolase class 2 (Gene Name=fbaA)

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