Structure of PDB 5qqy Chain B

Receptor sequence
>5qqyB (length=428) Species: 9606 (Homo sapiens) [Search protein sequence]
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSSKDV
SVWCSNDYLGMSRHPQVLQATQETLQRHGVGAGGTRNISGTSKFHVELEQ
ELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQG
IRNSGAAKFVFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLE
ELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGK
AFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGE
EGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALNSKLCD
LLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT
AVGLPLQCRRPVHFELMSEWERSYFGNM
3D structure
PDB5qqy PanDDA analysis group deposition
ChainB
Resolution1.49 Å
3D
structure
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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 S257 C258 F259 N262 H285 E328 D357 V359 H360 T388 K391 S116 C117 F118 N121 H144 E187 D216 V218 H219 T247 K250
BS02 NUG B E155 S573 Y574 E19 S423 Y424
BS03 PLP B T420 T421 T279 T280
BS04 NUG B K271 I272 Y413 K130 I131 Y272
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5qqy, PDBe:5qqy, PDBj:5qqy
PDBsum5qqy
PubMed
UniProtP22557|HEM0_HUMAN 5-aminolevulinate synthase, erythroid-specific, mitochondrial (Gene Name=ALAS2)

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