Structure of PDB 4gt2 Chain E

Receptor sequence
>4gt2E (length=370) Species: 100226 (Streptomyces coelicolor A3(2)) [Search protein sequence]
ATPLTSLGSERAMFHGKHQPGITTPMQARGHLVAFDLAAGAGRKEAAALL
RRWSDTARRLMAGEPAGSRDTDVARDAGPSSLTVTFGFGHSFFGRTGLEE
QRPVALDPLPDFSSDHLDKNRSNGDLWVQIGADDALVAFHALRAIQRDAG
AAARVRWQMNGFNRSPGATAHPMTARNLMGQVDGTRNPKPGEADFDRRIF
VPEEPAWMANGSYVVVRRIRMLLDDWEELSLKAQEDVIGRRKSDGAPLSG
GSGATESTEMDLEKTDGSGELVVPINAHARITRPDQNGGAAMVRRPFSYH
DGFDADGVPDAGLLFVCWQADPLRGFVPVQRKLDRGDALSQFIRHEASGL
FAVPGGAAEGEYVGQRLLEG
3D structure
PDB4gt2 DyP-type peroxidases from Stretptomyces and Thermobifida can modify organosolv lignin.
ChainE
Resolution1.8 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 E Q249 V250 G252 T253 R254 I294 H353 T357 R358 R369 F390 F401 V404 Q405 L408 L414 Q181 V182 G184 T185 R186 I219 H278 T282 R283 R294 F315 F326 V329 Q330 L333 L339
BS02 OXY E D251 R369 D183 R294
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4gt2, PDBe:4gt2, PDBj:4gt2
PDBsum4gt2
PubMed
UniProtQ9ZBW9

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