Structure of PDB 1pjq Chain B Binding Site BS01

Receptor Information
>1pjq Chain B (length=455) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLEAGARLTVNALTFIPQFT
VWANEGMLTLVEGPFDETLLDSCWLAIAATDDDTVNQRVSDAAESRRIFC
NVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQH
LGQVARYAGQLRARVKKQFATMGERRRFWEKFFVNDRLAQSLANADEKAV
NATTERLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRL
VSDDIMNLVRRDADRVFVGKRAHCVPQEEINQILLREAQKGKRVVRLKGG
DPFIFGRGGEELETLCHAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQS
VRLVTGHLKTGGELDWENLAAEKQTLVFYMGLNQAATIQEKLIAFGMQAD
MPVALVENGTSVKQRVVHGVLTQLGELAQQVESPALIIVGRVVALRDKLN
WFSNH
Ligand information
Ligand IDSAH
InChIInChI=1S/C14H20N6O5S/c15-6(14(23)24)1-2-26-3-7-9(21)10(22)13(25-7)20-5-19-8-11(16)17-4-18-12(8)20/h4-7,9-10,13,21-22H,1-3,15H2,(H,23,24)(H2,16,17,18)/t6-,7+,9+,10+,13+/m0/s1
InChIKeyZJUKTBDSGOFHSH-WFMPWKQPSA-N
SMILES
SoftwareSMILES
CACTVS 3.341N[CH](CCSC[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23)C(O)=O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)CSCCC(C(=O)O)N)O)O)N
CACTVS 3.341N[C@@H](CCSC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23)C(O)=O
ACDLabs 10.04O=C(O)C(N)CCSCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CSCC[C@@H](C(=O)O)N)O)O)N
FormulaC14 H20 N6 O5 S
NameS-ADENOSYL-L-HOMOCYSTEINE
ChEMBLCHEMBL418052
DrugBankDB01752
ZINCZINC000004228232
PDB chain1pjq Chain B Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1pjq CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis.
Resolution2.21 Å
Binding residue
(original residue number in PDB)		G301 D303 I306 F307 T331 A332 C336 Y381 M382 N410 G411 A437 L438
Binding residue
(residue number reindexed from 1)		G299 D301 I304 F305 T329 A330 C334 Y379 M380 N408 G409 A435 L436
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) D248 K270 M382
Catalytic site (residue number reindexed from 1) D248 K270 M380
Enzyme Commision number 1.3.1.76: precorrin-2 dehydrogenase.
2.1.1.107: uroporphyrinogen-III C-methyltransferase.
4.99.1.4: sirohydrochlorin ferrochelatase.
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
View graph for
Biological Process
External links
PDB RCSB:1pjq, PDBe:1pjq, PDBj:1pjq
PDBsum1pjq
PubMed14595395
UniProtP25924|CYSG_SALTY Siroheme synthase (Gene Name=cysG)

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