Structure of PDB 4htg Chain A

Receptor sequence
>4htgA (length=302) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
TAIIRIGTRGSPLALAQAYETREKLKKKHPELVEDGAIHIEIIKTTGDKI
LSQPLADIGGKGLFTKEIDEALINGHIDIAVHSMKDVPTYLPEKTILPCN
LPREDVRDAFICLTAATLAELPAGSVVGTASLRRKSQILHKYPALHVEEN
FRGNVQTRLSKLQGGKVQATLLALAGLKRLSMTENVASILSLDEMLPAVA
QGAIGIACRTDDDKMATYLASLNHEETRLAISCERAFLETLDGSCRTPIA
GYASKDEEGNCIFRGLVASPDGTKVLETSRKGPYVYEDMVKMGKDAGQEL
LS
3D structure
PDB4htg Insights into the mechanism of pyrrole polymerization catalysed by porphobilinogen deaminase: high-resolution X-ray studies of the Arabidopsis thaliana enzyme.
ChainA
Resolution1.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K94 D95 R142 R143 R161 R167 C254
Catalytic site (residue number reindexed from 1) K85 D86 R133 R134 R152 R158 C245
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 18W A R18 S20 L64 K94 D95 T138 A139 S140 R142 R143 R161 G162 N163 V164 R167 C254 R9 S11 L55 K85 D86 T129 A130 S131 R133 R134 R152 G153 N154 V155 R158 C245
Gene Ontology
Molecular Function
GO:0004418 hydroxymethylbilane synthase activity
Biological Process
GO:0018160 peptidyl-pyrromethane cofactor linkage
GO:0033014 tetrapyrrole biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4htg, PDBe:4htg, PDBj:4htg
PDBsum4htg
PubMed23519422
UniProtQ43316|HEM3_ARATH Porphobilinogen deaminase, chloroplastic (Gene Name=HEMC)

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