- PDB-1e51: Crystal structure of native human erythrocyte 5-aminolaevulinic a... -
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Basic information
Entry
Database: PDB / ID: 1.0E+51
Title
Crystal structure of native human erythrocyte 5-aminolaevulinic acid dehydratase
Components
DELTA-AMINOLEVULINIC ACID DEHYDRATASE
Keywords
LYASE / DEHYDRATASE / TETRAPYRROLE BIOSYNTHESIS / TIM BARREL / PORPHOBILINOGEN SYNTHASE / LEAD POISONING
Function / homology
Function and homology information
proteasome core complex binding / response to vitamin B1 / response to platinum ion / porphobilinogen synthase / porphobilinogen synthase activity / heme B biosynthetic process / heme O biosynthetic process / heme A biosynthetic process / negative regulation of proteasomal protein catabolic process / cellular response to lead ion ...proteasome core complex binding / response to vitamin B1 / response to platinum ion / porphobilinogen synthase / porphobilinogen synthase activity / heme B biosynthetic process / heme O biosynthetic process / heme A biosynthetic process / negative regulation of proteasomal protein catabolic process / cellular response to lead ion / response to mercury ion / response to aluminum ion / response to selenium ion / response to fatty acid / protoporphyrinogen IX biosynthetic process / response to cobalt ion / response to methylmercury / response to arsenic-containing substance / response to herbicide / response to iron ion / Heme biosynthesis / heme biosynthetic process / response to ionizing radiation / response to zinc ion / response to vitamin E / cellular response to interleukin-4 / response to amino acid / response to cadmium ion / catalytic activity / response to glucocorticoid / response to activity / protein homooligomerization / secretory granule lumen / response to ethanol / response to oxidative stress / ficolin-1-rich granule lumen / response to lipopolysaccharide / response to hypoxia / response to xenobiotic stimulus / Neutrophil degranulation / extracellular exosome / zinc ion binding / extracellular region / identical protein binding / nucleus / cytosol Similarity search - Function
Delta-aminolevulinic acid dehydratase / Delta-aminolevulinic acid dehydratase, active site / Delta-aminolevulinic acid dehydratase / Delta-aminolevulinic acid dehydratase active site. / Delta-aminolevulinic acid dehydratase / Aldolase class I / Aldolase-type TIM barrel / TIM Barrel / Alpha-Beta Barrel / Alpha Beta Similarity search - Domain/homology
Mass: 36338.852 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: PORPHOBILINOGEN IN ACTIVE SITE OF MONOMER A / Source: (natural) HOMO SAPIENS (human) / Cell: ERYTHROCYTES / References: UniProt: P13716, porphobilinogen synthase
Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
Compound details
PORPHOBILINOGEN PRODUCT MOLECULE BOUND AT MONOMER A ACTIVE SITE. SECOND STEP IN PORPHYRIN AND HEME ...PORPHOBILINOGEN PRODUCT MOLECULE BOUND AT MONOMER A ACTIVE SITE. SECOND STEP IN PORPHYRIN AND HEME BIOSYNTHESIS DISEASE: DEFECTS IN ALAD ARE THE CAUSE OF ACUTE HEPATIC PORPHYRIA CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + H(2)O COFACTOR: ZINC POLYMORPHISM: THERE ARE TWO COMMON ALLELES OF ALAD. INDIVIDUALS HETEROZYGOUS OR HOMOZYGOUS FOR THE 2ND ALLELE HAVE SIGNIFICANTLY HIGHER BLOOD LEAD LEVELS THAN DO 1ST ALLELE HOMOZYGOTES WHEN EXPOSED TO ENVIRONMENTAL LEAD.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.72 Å3/Da / Density % sol: 56 %
Resolution: 2.83→44.38 Å / Rfactor Rfree error: 0.009 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 Details: BREAK IN CHAIN A 137-138 DUE TO DISORDER. BREAKS IN CHAIN B 89-93, 127-142 AND 213-220 DUE TO DISORDER.
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