Structure of PDB 7aaj Chain B

Receptor sequence

>7aajB (length=324) Species: 9606 (Homo sapiens)

KMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSSLFTKELEH
ALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPHDAVVFHPKFVGKT
LETLPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQQEF
SAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILD
LVGVLHDPETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVW
SLDGSDSIQETMQATIHVPAQHEDGPEDDPQLVGITARNIPRGPQLAAQN
LGISLANLLLSKGAKNILDVARQL

3D structure

• PDB: 7aaj Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism.
• Chain: B
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K98 D99 R149 R150 R167 R173 C261
• Catalytic site (residue number reindexed from 1): K65 D66 R116 R117 R134 R140 C228
• 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	B	S96 K98 D99 S146 S147 R149 R150 R173 L188 A189 C261	S63 K65 D66 S113 S114 R116 R117 R140 L155 A156 C228

Gene Ontology

Molecular Function

• GO:0004418 hydroxymethylbilane synthase activity
• GO:0005515 protein binding
• 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:0006784 heme A biosynthetic process
• GO:0006785 heme B biosynthetic process
• GO:0018160 peptidyl-pyrromethane cofactor linkage
• GO:0033014 tetrapyrrole biosynthetic process
• GO:0048034 heme O biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:7aaj, PDBe:7aaj, PDBj:7aaj
• PDBsum: 7aaj
• PubMed: 33665570
• UniProt: P08397|HEM3_HUMAN Porphobilinogen deaminase (Gene Name=HMBS)