Structure of PDB 5lzl Chain E

Receptor sequence
>5lzlE (length=336) Species: 410359 (Pyrobaculum calidifontis JCM 11548) [Search protein sequence]
MRVQFPTTRPRRLRASKIIRDAVAETQIDAGDFIYPLFVKPGGEREPIGP
MPGIYRWPVGRELINHVEEALSLGINKFILFGVLPDELKNPEGTGGYDPE
GVVPRAIRLIKEIFGDRVLVFADVCLCEYTDHGHCGVVKEKRDRWYVDND
ETIKLYAKEAVVYAEAGADFVAPSGMMDGQVREIRRALDAHGFEEVGIMA
YSAKYASAFYGPFRVAAASAPKFGDRRTYQMDPRNAYEALKEVAMDLEEG
ADIVMVKPALAYLDVIRLVKQHFPWVPLAAYNVSGEYSLVKAAATAGYVD
ERTITLEILTAIKRAGADLILTYHALEAAKWIKEGL
3D structure
PDB5lzl Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis.
ChainE
Resolution3.47 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 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.
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 ZN E C125 C127 C125 C127
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5lzl, PDBe:5lzl, PDBj:5lzl
PDBsum5lzl
PubMed28045381
UniProtA3MWV9

[Back to BioLiP]