Structure of PDB 4mlq Chain A

Receptor sequence

>4mlqA (length=289) Species: 1404 (Priestia megaterium)

SHMRKIIVGSRRSKLALTQTKWVIEQLKKQGLPFEFEIKEMVKEIEQAML
DKEIDMAVHSMKDMPAVLPEGLTIGCIPLREDHRDALISKNGERFEELPS
GAVIGTSSLRRGAQLLSMRSDIEIKWIRGNIDTRLEKLKNEDYDAIILAA
AGLSRMGWSKDTVTQYLEPEISVPAVGQGALAIECRENDHELLSLLQALN
HDETARAVRAERVFLKEMEGGCQVPIAGYGRILDGGNIELTSLVASPDGK
TIYKEHITGKDPIAIGSEAAERLTSQGAKLLIDRVKEEL

3D structure

• PDB: 4mlq Structural evidence for the partially oxidized dipyrromethene and dipyrromethanone forms of the cofactor of porphobilinogen deaminase: structures of the Bacillus megaterium enzyme at near-atomic resolution.
• Chain: A
• Resolution: 1.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K81 D82 R129 R130 R147 R153 C241
• Catalytic site (residue number reindexed from 1): K62 D63 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 D82 T125 S126 S127 R129 R130 R153 A168 Q197 C241	S60 K62 D63 T106 S107 S108 R110 R111 R134 A149 Q178 C222
BS02	29P	A	R9 S11 K81 D82 T125 S126 S127 R129 R130 R147 G148 N149 R153 C241	R11 S13 K62 D63 T106 S107 S108 R110 R111 R128 G129 N130 R134 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

External links

• PDB: RCSB:4mlq, PDBe:4mlq, PDBj:4mlq
• PDBsum: 4mlq
• PubMed: 24598743
• UniProt: Q8GCA8