Structure of PDB 5m7f Chain B

Receptor sequence
>5m7fB (length=316) Species: 9606 (Homo sapiens) [Search protein sequence]
VIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSLFTKELEHALEK
NEVDLVVHSLKDLPTVLPPGFTIGAICKRENPHDAVVFHPKFVGKTLETL
PEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQQEFSAII
LATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGV
LHDPETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDG
SDSIQETMQATIHVPAQHEDGPEDDPQLVGITARNIPRGPQLAAQNLGIS
LANLLLSKGAKNILDV
3D structure
PDB5m7f Structural basis of pyrrole polymerization in human porphobilinogen deaminase.
ChainB
Resolution2.78 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) K61 D62 R112 R113 R130 R136 C224
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 R150 R173 L188 A189 R195 C261 S59 K61 D62 S109 S110 R113 R136 L151 A152 R158 C224
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:5m7f, PDBe:5m7f, PDBj:5m7f
PDBsum5m7f
PubMed29908816
UniProtP08397|HEM3_HUMAN Porphobilinogen deaminase (Gene Name=HMBS)

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