Structure of PDB 5vjd Chain A

Receptor sequence
>5vjdA (length=343) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
SKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTDSINAVLETAA
KVKAPVIVQFSNGGASFIAGKGVKSDVPQGAAILGAISGAHHVHQMAEHY
GVPVILHTDHCAKKLLPWIDGLLDAGEKHFAATGKPLFSSHMIDLSEESL
QENIEICSKYLERMSKIGMTLEIELGCTGGYTQPEDVDYAYTELSKISPR
FTIAASFGNVHGVYKPGNVVLTPTILRDSQEYVSKKHNLPHNSLNFVFHG
GSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVLNYYKANEAYLQGQLG
NPKGEDQPNKKYYDPRVWLRAGQTSMIARLEKAFQELNAIDVL
3D structure
PDB5vjd Active site remodeling during the catalytic cycle in metal-dependent fructose-1,6-bisphosphate aldolases.
ChainA
Resolution1.701 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 H226 H264 N286
Catalytic site (residue number reindexed from 1) D109 H110 H211 H249 N271
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 H226 H264 H110 H211 H249
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:5vjd, PDBe:5vjd, PDBj:5vjd
PDBsum5vjd
PubMed29593097
UniProtP0AB71|ALF_ECOLI Fructose-bisphosphate aldolase class 2 (Gene Name=fbaA)

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