Structure of PDB 5hms Chain B Binding Site BS01

Receptor Information
>5hms Chain B (length=328) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MQPQSVLHSGYFHPLLRAWQTATTTLNASNLIYPIFVTDVPDDIQPITSL
PGVARYGVKRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERGSAADSEESP
AIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFRAEESRQRL
AEVALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGLGNRVSVMSYSAKF
ASCFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLM
VKPGMPYLDIVREVKDKHPDLPLAVYHVSGEFAMLWHGAQAGAFDLKAAV
LEAMTAFRRAGADIIITYYTPQLLQWLK
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain5hms Chain B Residue 400 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5hms Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		C122 C124 C132
Binding residue
(residue number reindexed from 1)		C122 C124 C132
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K199 K252
Catalytic site (residue number reindexed from 1) K199 K252
Enzyme Commision number 4.2.1.24: porphobilinogen synthase.
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:5hms, PDBe:5hms, PDBj:5hms
PDBsum5hms
PubMed28045381
UniProtP13716|HEM2_HUMAN Delta-aminolevulinic acid dehydratase (Gene Name=ALAD)

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