Structure of PDB 7aaj Chain A

Receptor sequence
>7aajA (length=323) Species: 9606 (Homo sapiens) [Search protein sequence]
KMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSLFTKELEHA
LEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPHDAVVFHPKFVGKTL
ETLPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQQEFS
AIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDL
VGVLHDPETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWS
LDGSDSIQETMQATIHVPAQHEDGPEDDPQLVGITARNIPRGPQLAAQNL
GISLANLLLSKGAKNILDVARQL
3D structure
PDB7aaj Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K98 D99 R149 R150 R167 R173 C261
Catalytic site (residue number reindexed from 1) K64 D65 R115 R116 R133 R139 C227
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 S96 K98 D99 S146 S147 R149 R150 R173 A189 R195 Q217 C261 S62 K64 D65 S112 S113 R115 R116 R139 A155 R161 Q183 C227
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:7aaj, PDBe:7aaj, PDBj:7aaj
PDBsum7aaj
PubMed33665570
UniProtP08397|HEM3_HUMAN Porphobilinogen deaminase (Gene Name=HMBS)

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