Structure of PDB 4gt2 Chain A

Receptor sequence
>4gt2A (length=371) Species: 100226 (Streptomyces coelicolor A3(2)) [Search protein sequence]
ATPLTSLGSERAMFHGKHQPGITTPMQARGHLVAFDLAAGAGRKEAAALL
RRWSDTARRLMAGEPAGSRDTDVARDAGPSSLTVTFGFGHSFFGRTGLEE
QRPVALDPLPDFSSDHLDKNRSNGDLWVQIGADDALVAFHALRAIQRDAG
AAARVRWQMNGFNRSPGATAHPMTARNLMGQVDGTRNPKPGEADFDRRIF
VPEEGPAWMANGSYVVVRRIRMLLDDWEELSLKAQEDVIGRRKSDGAPLS
GGSGATESTEMDLEKTDGSGELVVPINAHARITRPDQNGGAAMVRRPFSY
HDGFDADGVPDAGLLFVCWQADPLRGFVPVQRKLDRGDALSQFIRHEASG
LFAVPGGAAEGEYVGQRLLEG
3D structure
PDB4gt2 DyP-type peroxidases from Stretptomyces and Thermobifida can modify organosolv lignin.
ChainA
Resolution1.8 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 Q249 V250 G252 T253 R254 I294 H353 T357 R358 R369 F390 F401 V404 Q405 L408 L414 Q181 V182 G184 T185 R186 I220 H279 T283 R284 R295 F316 F327 V330 Q331 L334 L340
BS02 OXY A D251 R369 D183 R295
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

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

[Back to BioLiP]