Structure of PDB 7snm Chain D

Receptor sequence
>7snmD (length=439) Species: 243233 (Methylococcus capsulatus str. Bath) [Search protein sequence]
SNTPPVKPGGLPLLGHILEFGKNPHAFLMALRHEFGDVAEFRMFHQRMVL
LTGSQASEAFYRAPDEVLDQGPAYRIMTPIFGRGVVFDARIERKNQQLQM
LMPALRDKPMRTYSEIIVAEVEAMLRDWKDAGTIDLLELTKELTIYTSSH
CLLGAEFRHELNTEFAGIYRDLEMGIQPIAYVFPNLPLPVFKRRDQARVR
LQELVTQIMERRARSQEVFQMLIDASYDDGSKLTPHEITGMLIATIFAGH
HTSSGTTAWVLIELLRRPEYLRRVRAEIDALFETHGRVTFESLRQMPQLE
NVIKEVLRLHPPLILLMRKVMKDFEVQGMRIEAGKFVCAAPSVTHRIPEL
FPNPELFDPDRYTPERAEDKDLYGWQAFGGGRHKCSGNAFAMFQIKAIVC
VLLRNYEFELAAAPESYRDDYRKMVVEPASPCLIRYRRR
3D structure
PDB7snm Unravelling the role of transient redox partner complexes in P450 electron transfer mechanics.
ChainD
Resolution2.55 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.13.70: Transferred entry: 1.14.14.154.
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 Q75 Y79 A257 T261 P321 R327 A386 F387 H392 C394 S395 G396 Q70 Y74 A248 T252 P312 R318 A377 F378 H383 C385 S386 G387
BS02 LAN D Y79 M82 F86 L103 Y186 A253 T254 A257 L324 Y74 M77 F81 L98 Y181 A244 T245 A248 L315
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016491 oxidoreductase activity
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:7snm, PDBe:7snm, PDBj:7snm
PDBsum7snm
PubMed36171457
UniProtQ603T8

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