Structure of PDB 1jcj Chain B

Receptor sequence
>1jcjB (length=251) Species: 562 (Escherichia coli) [Search protein sequence]
HMTDLKASSLRALKLMDLTTLNDDDTDEKVIALCHQAKTPVGNTAAICIY
PRFIPIARKTLKEQGTPEIRIATVTNFPHGNDDIDIALAETRAAIAYGAD
EVDVVFPYRALMAGNEQVGFDLVKACKEACAAANVLLKVIIETGELKDEA
LIRKASEISIKAGADFIKTSTGKVAVNATPESARIMMEVIRDMGVEKTVG
FLPAGGVRTAEDAQKYLAIADELFGADWADARHYRFGASSLLASLLKALG
H
3D structure
PDB1jcj Observation of covalent intermediates in an enzyme mechanism at atomic resolution.
ChainB
Resolution1.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D102 K167 L201
Catalytic site (residue number reindexed from 1) D103 K168 L202
Enzyme Commision number 4.1.2.4: deoxyribose-phosphate 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 HPD B K167 T170 G204 G236 A237 S238 K168 T171 G205 G237 A238 S239
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004139 deoxyribose-phosphate aldolase activity
GO:0016829 lyase activity
Biological Process
GO:0006018 2-deoxyribose 1-phosphate catabolic process
GO:0006974 DNA damage response
GO:0009264 deoxyribonucleotide catabolic process
GO:0015949 nucleobase-containing small molecule interconversion
GO:0016052 carbohydrate catabolic process
GO:0046386 deoxyribose phosphate catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1jcj, PDBe:1jcj, PDBj:1jcj
PDBsum1jcj
PubMed11598300
UniProtP0A6L0|DEOC_ECOLI Deoxyribose-phosphate aldolase (Gene Name=deoC)

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