Structure of PDB 5qqy Chain A

Receptor sequence
>5qqyA (length=429) Species: 9606 (Homo sapiens) [Search protein sequence]
LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSKDVS
VWCSNDYLGMSRHPQVLQATQETLQRHGVGAGGTRNISGTSKFHVELEQE
LAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGI
RNSGAAKFVFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEE
LCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKA
FGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEE
GQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALNSKLCDL
LLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA
VGLPLQNFCRRPVHFELMSEWERSYFGNM
3D structure
PDB5qqy PanDDA analysis group deposition
ChainA
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 A T420 T421 T278 T279
BS02 NUG A K271 Y413 K129 Y271
BS03 PLP A S257 C258 F259 H285 E328 S332 D357 V359 H360 T388 K391 S115 C116 F117 H143 E186 S190 D215 V217 H218 T246 K249
BS04 NUG A K152 E155 S573 Y574 K16 E19 S424 Y425
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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