Structure of PDB 1pjt Chain A

Receptor sequence
>1pjtA (length=448) [Search protein sequence]
MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLEAGARLTVNALTFIPQFT
VWANEGMLTLVEGPFDETLLDSCWLAIAATDDDTVNQRVSDAAESRRIFC
NVVDAPKAASFIMPSIIDRSPLMVAVSAGGTSPVLARLLREKLESLLPQH
LGQVARYAGQLRARVKKQFATMGERRRFWEKFFVNDRLAQSLANADEKAV
NATTERLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRL
VSDDIMNLVRRDADRVFVGKRHCVPQEEINQILLREAQKGKRVVRLKGGD
PFIFGRGGEELETLCHAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSV
RLVTGELDWENLAAEKQTLVFYMGLNQAATIQEKLIAFGMQADMPVALVE
NGTSVKQRVVHGVLTQLGELAQQVESPALIIVGRVVALRDKLNWFSNH
3D structure
PDB1pjt CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis.
ChainA
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 A P225 G301 G302 D303 I306 F307 T331 A332 C336 Y381 P436 A437 P225 G298 G299 D300 I303 F304 T328 A329 C333 Y372 P427 A428
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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