Structure of PDB 3ecr Chain A

Receptor sequence
>3ecrA (length=318) Species: 9606 (Homo sapiens) [Search protein sequence]
MRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMLFTKELEHALE
KNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPHDAVVFHPKFVGKTLET
LPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQQEFSAI
ILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVG
VLHDPETLLRCIAERAFLRHLECSVPVAVHTAMKDGQLYLTGGVWSLDGS
DSIQETMQATIHVPAQHEDGPEDDPQLVGITARNIPRGPQLAAQNLGISL
ANLLLSKGAKNILDVARQ
3D structure
PDB3ecr Structural insight into acute intermittent porphyria.
ChainA
Resolution2.182 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K101 D102 R152 R153 R170 R176 C264
Catalytic site (residue number reindexed from 1) K62 D63 R113 R114 R131 R137 C223
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 S99 K101 D102 S150 R152 R153 R176 L191 A192 A217 Q220 G221 C264 S60 K62 D63 S111 R113 R114 R137 L152 A153 A178 Q181 G182 C223
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:3ecr, PDBe:3ecr, PDBj:3ecr
PDBsum3ecr
PubMed18936296
UniProtP08397|HEM3_HUMAN Porphobilinogen deaminase (Gene Name=HMBS)

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