Structure of PDB 4gt2 Chain E Binding Site BS02

Receptor Information

>4gt2 Chain E (length=370) Species: 100226 (Streptomyces coelicolor A3(2)) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

ATPLTSLGSERAMFHGKHQPGITTPMQARGHLVAFDLAAGAGRKEAAALL
RRWSDTARRLMAGEPAGSRDTDVARDAGPSSLTVTFGFGHSFFGRTGLEE
QRPVALDPLPDFSSDHLDKNRSNGDLWVQIGADDALVAFHALRAIQRDAG
AAARVRWQMNGFNRSPGATAHPMTARNLMGQVDGTRNPKPGEADFDRRIF
VPEEPAWMANGSYVVVRRIRMLLDDWEELSLKAQEDVIGRRKSDGAPLSG
GSGATESTEMDLEKTDGSGELVVPINAHARITRPDQNGGAAMVRRPFSYH
DGFDADGVPDAGLLFVCWQADPLRGFVPVQRKLDRGDALSQFIRHEASGL
FAVPGGAAEGEYVGQRLLEG

Ligand information

InChI=1S/O2/c1-2

MYMOFIZGZYHOMD-UHFFFAOYSA-N

SMILES

Software	SMILES
CACTVS 3.341 OpenEye OEToolkits 1.5.0	O=O

Formula

Name

OXYGEN MOLECULE

PDB chain

4gt2 Chain E Residue 504 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	4gt2 DyP-type peroxidases from Stretptomyces and Thermobifida can modify organosolv lignin.
Resolution	1.8 Å
Binding residue (original residue number in PDB)	D251 R369
Binding residue (residue number reindexed from 1)	D183 R294
Annotation score	1

Enzymatic activity

Enzyme Commision number

1.11.1.-
4.98.1.1: protoporphyrin ferrochelatase.

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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Cellular Component

External links

PDB	RCSB:4gt2, PDBe:4gt2, PDBj:4gt2
PDBsum	4gt2
PubMed
UniProt	Q9ZBW9

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