Structure of PDB 4egn Chain D

Receptor sequence
>4egnD (length=393) Species: 316058 (Rhodopseudomonas palustris HaA2) [Search protein sequence]
TIPHLAIDPFSLDFFDDPYPDQQTLRDAGPVVYLDKWNVYGVARYAEVHA
VLNDPTTFCSSRGVGLSDFKKEKPWRPPSLILEADPPAHTRPRAVLSKVL
SPATMKTIRDGFAAAADAKVDELLQRGCIDAIADLAEAYPLSVFPDAMGL
KQEGREHLLPYAGLVFNAFGPPNELRQTAIERSAPHQAYVNEQCQRPNLA
PGGFGACIHAFTDTGEITPDEAPLLVRSLLSAGLDTTVNGIGAAVYCLAR
FPGELQRLRSDPTLARNAFEEAVRFESPVQTFFRTTTREVELGGAVIGEG
EKVLMFLGSANRDPRRWSDPDLYDITRKTSGHVGFGSGVHMCVGQLVARL
EGEVMLSALARKVAAIDIDGPVKRRFNNTLRGLESLPVKLTPA
3D structure
PDB4egn Investigation of the substrate range of CYP199A4: modification of the partition between hydroxylation and desaturation activities by substrate and protein engineering
ChainD
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N183 A248 D251 T252 T253 C358 V359 G360 E367 L396
Catalytic site (residue number reindexed from 1) N167 A232 D235 T236 T237 C342 V343 G344 E351 L380
Enzyme Commision number ?
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 D I97 L98 H105 R109 A248 G249 T252 F298 R300 G350 F351 H356 C358 V359 G360 A364 I81 L82 H89 R93 A232 G233 T236 F282 R284 G334 F335 H340 C342 V343 G344 A348
BS02 TWO D S95 L98 V181 F182 F185 S244 S247 A248 F298 S79 L82 V165 F166 F169 S228 S231 A232 F282 MOAD: Kd=29.5uM
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:4egn, PDBe:4egn, PDBj:4egn
PDBsum4egn
PubMed23135838
UniProtQ2IU02

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