Structure of PDB 1e51 Chain A

Receptor sequence
>1e51A (length=326) Species: 9606 (Homo sapiens) [Search protein sequence]
MQPQSVLHSGYFHPLLRAWQTATTTLNASNLIYPIFVTDVPDDIQPITSL
PGVARYGVKRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERGSAADSEESP
AIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSGAFRAEESRQRLAE
VALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGLGNRVSVMSYSAKFAS
CFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLMVK
PGMPYLDIVREVKDKHPDLPLAVYHVSGEFAMLWHGAQAGAFDLKAAVLE
AMTAFRRAGADIIITYYTPQLLQWLK
3D structure
PDB1e51 The Crystal Structure of Human Ala-Dehydratase
ChainA
Resolution2.83 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K199 K252
Catalytic site (residue number reindexed from 1) K197 K250
Enzyme Commision number 4.2.1.24: porphobilinogen synthase.
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 PBG A C124 S168 K199 Y205 F208 R209 R221 Q225 K252 V278 S279 Y318 C124 S166 K197 Y203 F206 R207 R219 Q223 K250 V276 S277 Y316
BS02 ZN A C124 C132 C124 C132
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004655 porphobilinogen synthase activity
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:1904854 proteasome core complex binding
Biological Process
GO:0001666 response to hypoxia
GO:0006782 protoporphyrinogen IX biosynthetic process
GO:0006783 heme biosynthetic process
GO:0006784 heme A biosynthetic process
GO:0006785 heme B biosynthetic process
GO:0006979 response to oxidative stress
GO:0007584 response to nutrient
GO:0009410 response to xenobiotic stimulus
GO:0009635 response to herbicide
GO:0009636 response to toxic substance
GO:0009725 response to hormone
GO:0010038 response to metal ion
GO:0010039 response to iron ion
GO:0010043 response to zinc ion
GO:0010044 response to aluminum ion
GO:0010212 response to ionizing radiation
GO:0010266 response to vitamin B1
GO:0010269 response to selenium ion
GO:0010288 response to lead ion
GO:0014070 response to organic cyclic compound
GO:0014823 response to activity
GO:0031667 response to nutrient levels
GO:0032025 response to cobalt ion
GO:0032496 response to lipopolysaccharide
GO:0033014 tetrapyrrole biosynthetic process
GO:0033197 response to vitamin E
GO:0033273 response to vitamin
GO:0043200 response to amino acid
GO:0045471 response to ethanol
GO:0046685 response to arsenic-containing substance
GO:0046686 response to cadmium ion
GO:0046689 response to mercury ion
GO:0048034 heme O biosynthetic process
GO:0051260 protein homooligomerization
GO:0051384 response to glucocorticoid
GO:0051597 response to methylmercury
GO:0070541 response to platinum ion
GO:0070542 response to fatty acid
GO:0071284 cellular response to lead ion
GO:0071353 cellular response to interleukin-4
GO:1901799 negative regulation of proteasomal protein catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005829 cytosol
GO:0034774 secretory granule lumen
GO:0070062 extracellular exosome
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1e51, PDBe:1e51, PDBj:1e51
PDBsum1e51
PubMed
UniProtP13716|HEM2_HUMAN Delta-aminolevulinic acid dehydratase (Gene Name=ALAD)

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