Structure of PDB 1olt Chain A

Receptor sequence
>1oltA (length=434) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
QQIDWDLALIKYYTSYPTALEFSEDFGEQAFLQAVARYPERPLSLYVHIP
FCHKLCYFCGCNKIVTRQQHKADQYLDALEQEIVHRAPLFAGRHVSQLHW
GGGTPTYLNKAQISRLMKLLRENFQFNADAEISIEVDPREIELDVLDHLR
AEGFNRLSMGVQDFNKEVQRLVNREQDEEFIFALLNHAREIGFTSTNIDL
IYGLPKQTPESFAFTLKRVAELNPDRLSVFNYAHLPTIFAAQRKIKDADL
PSPQQKLDILQETIAFLTQSGYQFIGMDHFARPDDELAVAQREGVLHRNF
QGYTTQGDTDLLGMGVSAISMIGDCYAQNQKELKQYYQQVDEQGNALWRG
IALTRDDCIRRDVIKSLICNFRLDYSPIEQQWDLLFADYFAEDLKLLAPL
AKDGLVDVDEKGIQVTAKGRLLIRNICMCFDTYL
3D structure
PDB1olt Crystal Structure of Coproporphyrinogen III Oxidase Reveals Cofactor Geometry of Radical Sam Enzymes
ChainA
Resolution2.07 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.3.98.3: coproporphyrinogen dehydrogenase.
Interaction with ligand
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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