Structure of PDB 5qqz Chain B

Receptor sequence
>5qqzB (length=428) Species: 9606 (Homo sapiens) [Search protein sequence]
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSSKDV
SVWCSNDYLGMSRHPQVLQATQETLQRHGVGAGGTRNISGTSKFHVELEQ
ELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQG
IRNSGAAKFVFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLE
ELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGK
AFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGE
EGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALNSKLCD
LLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT
AVGLPLQCRRPVHFELMSEWERSYFGNM
3D structure
PDB5qqz PanDDA analysis group deposition
ChainB
Resolution1.55 Å
3D
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
Enzyme Commision number 2.3.1.37: 5-aminolevulinate 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 PLP B C258 F259 N262 H285 E328 D357 V359 H360 K391 C117 F118 N121 H144 E187 D216 V218 H219 K250
BS02 NUJ B W171 D190 W35 D49
BS03 PLP B T420 T421 T279 T280
Gene Ontology
Molecular Function
GO:0003870 5-aminolevulinate synthase activity
GO:0016740 transferase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0009058 biosynthetic process
GO:0033014 tetrapyrrole biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5qqz, PDBe:5qqz, PDBj:5qqz
PDBsum5qqz
PubMed
UniProtP22557|HEM0_HUMAN 5-aminolevulinate synthase, erythroid-specific, mitochondrial (Gene Name=ALAS2)

[Back to BioLiP]