Structure of PDB 1olt Chain A Binding Site BS01

Receptor Information
>1olt Chain A (length=434) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QQIDWDLALIKYYTSYPTALEFSEDFGEQAFLQAVARYPERPLSLYVHIP
FCHKLCYFCGCNKIVTRQQHKADQYLDALEQEIVHRAPLFAGRHVSQLHW
GGGTPTYLNKAQISRLMKLLRENFQFNADAEISIEVDPREIELDVLDHLR
AEGFNRLSMGVQDFNKEVQRLVNREQDEEFIFALLNHAREIGFTSTNIDL
IYGLPKQTPESFAFTLKRVAELNPDRLSVFNYAHLPTIFAAQRKIKDADL
PSPQQKLDILQETIAFLTQSGYQFIGMDHFARPDDELAVAQREGVLHRNF
QGYTTQGDTDLLGMGVSAISMIGDCYAQNQKELKQYYQQVDEQGNALWRG
IALTRDDCIRRDVIKSLICNFRLDYSPIEQQWDLLFADYFAEDLKLLAPL
AKDGLVDVDEKGIQVTAKGRLLIRNICMCFDTYL
Ligand information
Ligand IDSF4
InChIInChI=1S/4Fe.4S
InChIKeyLJBDFODJNLIPKO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7[S]12[Fe]3[S]4[Fe]1[S]5[Fe]2[S]3[Fe]45
CACTVS 3.385S1[Fe]S[Fe]1.S2[Fe]S[Fe]2
FormulaFe4 S4
NameIRON/SULFUR CLUSTER
ChEMBL
DrugBank
ZINC
PDB chain1olt Chain A Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1olt Crystal Structure of Coproporphyrinogen III Oxidase Reveals Cofactor Geometry of Radical Sam Enzymes
Resolution2.07 Å
Binding residue
(original residue number in PDB)
C62 C66 F68 C69 K73 G113 T114 R184
Binding residue
(residue number reindexed from 1)
C52 C56 F58 C59 K63 G103 T104 R174
Annotation score1
Enzymatic activity
Enzyme Commision number 1.3.98.3: coproporphyrinogen dehydrogenase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004109 coproporphyrinogen oxidase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
GO:0051989 coproporphyrinogen dehydrogenase activity
Biological Process
GO:0006779 porphyrin-containing compound biosynthetic process
GO:0006782 protoporphyrinogen IX biosynthetic process
GO:0019353 protoporphyrinogen IX biosynthetic process from glutamate
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1olt, PDBe:1olt, PDBj:1olt
PDBsum1olt
PubMed14633981
UniProtP32131|HEMN_ECOLI Oxygen-independent coproporphyrinogen III oxidase (Gene Name=hemN)

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