Structure of PDB 1pda Chain A

Receptor sequence
>1pdaA (length=296) Species: 562 (Escherichia coli) [Search protein sequence]
DNVLRIATRQSPLALWQAHYVKDKLMASHPGLVVELVPMVTRGDVIGKGL
FVKELEVALLENRADIAVHSMKDVPVEFPQGLGLVTICEREDPRDAFVSN
NYDSLDALPAGSIVGTSSLRRQCQLAERRPDLIIRSLRGNVGTRLSKLDN
GEYDAIILAVAGLKRLGLESRIRAALPPEISLPAVGQGAVGIECRLDDSR
TRELLAALNHHETALRVTAERAMNTRLEGACQVPIGSYAELIDGEIWLRG
LVGAPDGSQIIRGERRGAPQDAEQMGISLAEELLNNGAREILAEVY
3D structure
PDB1pda Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site.
ChainA
Resolution1.76 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K83 D84 R131 R132 R149 R155 C242
Catalytic site (residue number reindexed from 1) K72 D73 R120 R121 R138 R144 C231
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 R11 S13 F62 K83 D84 T127 S128 S129 R131 R132 R149 G150 N151 V152 R155 C242 R9 S11 F51 K72 D73 T116 S117 S118 R120 R121 R138 G139 N140 V141 R144 C231
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
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:1pda, PDBe:1pda, PDBj:1pda
PDBsum1pda
PubMed1522882
UniProtP06983|HEM3_ECOLI Porphobilinogen deaminase (Gene Name=hemC)

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