Structure of PDB 5hnr Chain A Binding Site BS01

Receptor Information

>5hnr Chain A (length=326) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

MQPQSVLHSGYFHPLLRAWQTATTTLNASNLIYPIFVTDVPDDIQPITSL
PGVARYGVKRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERGSAADSEESP
AIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSGAFRAEESRQRLAE
VALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGLGNRVSVMSYSAKFAS
CFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLMVK
PGMPYLDIVREVKDKHPDLPLAVYHVSGEFAMLWHGAQAGAFDLKAAVLE
AMTAFRRAGADIIITYYTPQLLQWLK

Ligand information

Ligand ID

InChI

InChI=1S/Zn/q+2

InChIKey

PTFCDOFLOPIGGS-UHFFFAOYSA-N

SMILES

Software	SMILES
CACTVS 3.341	[Zn++]
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Zn+2]

Formula

Name

ZINC ION

PDB chain

5hnr Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	5hnr Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis.
Resolution	2.83 Å
Binding residue (original residue number in PDB)	C122 C124 C132
Binding residue (residue number reindexed from 1)	C122 C124 C132
Annotation score	1

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.

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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External links

PDB	RCSB:5hnr, PDBe:5hnr, PDBj:5hnr
PDBsum	5hnr
PubMed	28045381
UniProt	P13716\|HEM2_HUMAN Delta-aminolevulinic acid dehydratase (Gene Name=ALAD)

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