Structure of PDB 5lzl Chain K Binding Site BS01

Receptor Information

>5lzl Chain K (length=336) Species: 410359 (Pyrobaculum calidifontis JCM 11548)

MRVQFPTTRPRRLRASKIIRDAVAETQIDAGDFIYPLFVKPGGEREPIGP
MPGIYRWPVGRELINHVEEALSLGINKFILFGVLPDELKNPEGTGGYDPE
GVVPRAIRLIKEIFGDRVLVFADVCLCEYTDHGHCGVVKEKRDRWYVDND
ETIKLYAKEAVVYAEAGADFVAPSGMMDGQVREIRRALDAHGFEEVGIMA
YSAKYASAFYGPFRVAAASAPKFGDRRTYQMDPRNAYEALKEVAMDLEEG
ADIVMVKPALAYLDVIRLVKQHFPWVPLAAYNVSGEYSLVKAAATAGYVD
ERTITLEILTAIKRAGADLILTYHALEAAKWIKEGL

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 5lzl Chain K Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5lzl Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis.
• Resolution: 3.47 Å
• Binding residue (original residue number in PDB): C125 C127
• Binding residue (residue number reindexed from 1): C125 C127
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): K204 K257
• Catalytic site (residue number reindexed from 1): K204 K257
• Enzyme Commision number: 4.2.1.24: porphobilinogen synthase.

Gene Ontology

Molecular Function

• GO:0004655 porphobilinogen synthase activity
• GO:0008270 zinc ion binding
• GO:0016829 lyase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006782 protoporphyrinogen IX biosynthetic process
• GO:0006783 heme biosynthetic process
• GO:0033014 tetrapyrrole biosynthetic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:5lzl, PDBe:5lzl, PDBj:5lzl
• PDBsum: 5lzl
• PubMed: 28045381
• UniProt: A3MWV9