Structure of PDB 1pjt Chain B

Receptor sequence
>1pjtB (length=455) [Search protein sequence]
MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLEAGARLTVNALTFIPQFT
VWANEGMLTLVEGPFDETLLDSCWLAIAATDDDTVNQRVSDAAESRRIFC
NVVDAPKAASFIMPSIIDRSPLMVAVSAGGTSPVLARLLREKLESLLPQH
LGQVARYAGQLRARVKKQFATMGERRRFWEKFFVNDRLAQSLANADEKAV
NATTERLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRL
VSDDIMNLVRRDADRVFVGKRAHCVPQEEINQILLREAQKGKRVVRLKGG
DPFIFGRGGEELETLCHAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQS
VRLVTGHLKTGGELDWENLAAEKQTLVFYMGLNQAATIQEKLIAFGMQAD
MPVALVENGTSVKQRVVHGVLTQLGELAQQVESPALIIVGRVVALRDKLN
WFSNH
3D structure
PDB1pjt CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis.
ChainB
Resolution2.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.3.1.76: precorrin-2 dehydrogenase.
2.1.1.107: uroporphyrinogen-III C-methyltransferase.
4.99.1.4: sirohydrochlorin ferrochelatase.
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 SAH B P225 L250 G301 G302 D303 I306 F307 T331 A332 C336 Y381 M382 G411 P436 A437 L438 P225 L250 G299 G300 D301 I304 F305 T329 A330 C334 Y379 M380 G409 P434 A435 L436
Gene Ontology
Molecular Function
GO:0004325 ferrochelatase activity
GO:0004851 uroporphyrin-III C-methyltransferase activity
GO:0008168 methyltransferase activity
GO:0016491 oxidoreductase activity
GO:0016829 lyase activity
GO:0043115 precorrin-2 dehydrogenase activity
GO:0051266 sirohydrochlorin ferrochelatase activity
GO:0051287 NAD binding
Biological Process
GO:0006779 porphyrin-containing compound biosynthetic process
GO:0009236 cobalamin biosynthetic process
GO:0019354 siroheme biosynthetic process
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:1pjt, PDBe:1pjt, PDBj:1pjt
PDBsum1pjt
PubMed14595395
UniProtP25924|CYSG_SALTY Siroheme synthase (Gene Name=cysG)

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