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Structure of PDB 2ij7 Chain D

Receptor sequence >2ij7D (length=391) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence] LLEVPFSARGDRIPDAVAELRTREPIRKVRTITGAEAWLVSSYALCTQVL EDRRFSMKETAAAGAPRLNALTVPPEVVNNMGNIADAGLRKAVMKAITPK APGLEQFLRDTANSLLDNLITEGAPADLRNDFADPLATALHCKVLGIPQE DGPKLFRSLSIAFMSSADPIPAAKINWDRDIEYMAGILENPNITTGLMGE LSRLRKDPAYSHVSDELFATIGVTFFGAGVISTGSFLTTALISLIQRPQL RNLLHEKPELIPAGVEELLRINLSFADGLPRLATADIQVGDVLVRKGELV LVLLEGANFDPEHFPNPGSIELDRPNPTSHLAFGRGQHFCPGSALGRRHA QIGIEALLKKMPGVDLAVPIDQLVWRTRFQRRIPERLPVLW

3D structure PDB 2ij7 Crystal structure of the Mycobacterium tuberculosis P450 CYP121-fluconazole complex reveals new azole drug-P450 binding mode. Chain D Resolution 1.9 Å 3D structure Catalytic site residues are labeled in the 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 Catalytic site (original residue number in PDB) S170 A233 I236 S237 T238 C345 P346 G347 H354 R386 Catalytic site (residue number reindexed from 1) S165 A228 I231 S232 T233 C340 P341 G342 H349 R381 Enzyme Commision number 1.14.19.70: mycocyclosin synthase.

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 M62 M86 H146 F230 G234 S237 T238 F241 F280 L284 R286 A337 F338 H343 C345 P346 G347 M57 M81 H141 F225 G229 S232 T233 F236 F275 L279 R281 A332 F333 H338 C340 P341 G342 BS02 TPF D T229 A233 S237 Q385 T224 A228 S232 Q380 MOAD: Kd=5uM BindingDB: Kd=6000nM

Gene Ontology Molecular Function GO:0004497 monooxygenase activity GO:0005506 iron ion binding GO:0008395 steroid hydroxylase activity GO:0009975 cyclase activity GO:0016491 oxidoreductase activity GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen GO:0016717 oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water GO:0020037 heme binding GO:0036199 cholest-4-en-3-one 26-monooxygenase activity GO:0046872 metal ion binding GO:0070025 carbon monoxide binding

	Biological Process
GO:0006707	cholesterol catabolic process

	Cellular Component
GO:0005737	cytoplasm

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