Structure of PDB 3o72 Chain A

Receptor sequence
>3o72A (length=375) Species: 544404 (Escherichia coli O157:H7 str. TW14359) [Search protein sequence]
VARNEKQPFYGEHQAGILTPQQAAMMLVAFDVLASDKADLERLFRLLTQR
FAFLTQGGAAPETPNPRLPPLDSGILGGYIAPDNLTITLSVGHSLFDERF
GLAPQMPKKLQKMTRFPNDSLDAALCHGDVLLQICANTQDTVIHALRDII
KHTPDLLSVRWKREGFISDHAARSKGKETPINLLGFKDGTANPDSQNDKL
MQKVVWVTADQQEPAWTIGGSYQAVRLIQFRVEFWDRTPLKEQQTIFGRD
KQTGAPLGMQHEHDVPDYASDPEGKGIALDSHIRLANPRTAESESSLMLR
RGYSYSLGVTNSGQLDMGLLFVCYQHDLEKGFLTVQKRLNGEALEEYVKP
IGGGYFFALPGVKDANDYLGSALLR
3D structure
PDB3o72 Crystal structure and biochemical features of EfeB/YcdB from Escherichia coli O157: ASP235 plays divergent roles in different enzyme-catalyzed processes
ChainA
Resolution1.95 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.11.1.-
4.98.1.1: protoporphyrin 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 HEM A K234 D235 G236 T237 A238 I275 F294 H329 A333 N334 R336 R347 L366 F368 F379 V382 L386 K187 D188 G189 T190 A191 I228 F247 H282 A286 N287 R289 R300 L319 F321 F332 V335 L339
BS02 OXY A D235 R347 D188 R300
Gene Ontology
Molecular Function
GO:0004325 ferrochelatase activity
GO:0004601 peroxidase activity
GO:0016829 lyase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0033212 iron import into cell
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005829 cytosol
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3o72, PDBe:3o72, PDBj:3o72
PDBsum3o72
PubMed21324904
UniProtQ8XAS4|EFEB_ECO57 Deferrochelatase (Gene Name=efeB)

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