Structure of PDB 5ov5 Chain A

Receptor sequence
>5ov5A (length=290) Species: 1404 (Priestia megaterium) [Search protein sequence]
HMRKIIVGSRRSKLALTQTKWVIEQLKKQGLPFEFEIKEMFVKEIEQAML
DKEIDMAVHSMKEMPAVLPEGLTIGCIPLREDHRDALISKNGERFEELPS
GAVIGTSSLRRGAQLLSMRSDIEIKWIRGNIDTRLEKLKNEDYDAIILAA
AGLSRMGWSKDTVTQYLEPEISVPAVGQGALAIECRENDHELLSLLQALN
HDETARAVRAERVFLKEMEGGCQVPIAGYGRILDGGNIELTSLVASPDGK
TIYKEHITGKDPIAIGSEAAERLTSQGAKLLIDRVKEELD
3D structure
PDB5ov5 Structural studies of domain movement in active-site mutants of porphobilinogen deaminase from Bacillus megaterium.
ChainA
Resolution1.81 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K81 E82 R129 R130 R147 R153 C241
Catalytic site (residue number reindexed from 1) K62 E63 R110 R111 R128 R134 C222
Enzyme Commision number 2.5.1.61: hydroxymethylbilane 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 DPM A S79 K81 E82 T125 S126 S127 R129 R130 R153 L167 A168 C241 S60 K62 E63 T106 S107 S108 R110 R111 R134 L148 A149 C222
Gene Ontology
Molecular Function
GO:0004418 hydroxymethylbilane synthase activity
GO:0016740 transferase activity
Biological Process
GO:0006779 porphyrin-containing compound biosynthetic process
GO:0006782 protoporphyrinogen IX biosynthetic process
GO:0006783 heme biosynthetic process
GO:0018160 peptidyl-pyrromethane cofactor linkage
GO:0033014 tetrapyrrole biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5ov5, PDBe:5ov5, PDBj:5ov5
PDBsum5ov5
PubMed29095155
UniProtQ8GCA8

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