Structure of PDB 6t0j Chain A Binding Site BS01

Receptor Information
>6t0j Chain A (length=429) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HMGLNTAIATRVNGTPPPEVPIADIELGSLDFWALDDDVRDGAFATLRRE
APISFWPTIELPGFVAGNGHWALTKYDDVFYASRHPDIFSSYPNITINDQ
TPELAEYFGSMIVLDDPRHQRLRSIVSRAFTPKVVARIEAAVRDRAHRLV
SSMIANNPDRQADLVSELAGPLPLQIICDMMGIPKADHQRIFHWTNVILG
FGDPDLATDFDEFMQVSADIGAYATALAEDRRVNHHDDLTSSLVEAEVDG
ERLSSREIASFFILLVVAGNETTRNAITHGVLALSRYPEQRDRWWSDFDG
LAPTAVEEIVRWASPVVYMRRTLTQDIELRGTKMAAGDKVSLWYCSANRD
ESKFADPWTFDLARNPNPHLGFGGGGAHFCLGANLARREIRVAFDELRRQ
MPDVVATEEPARLLSQFIHGIKTLPVTWS
Ligand information
Ligand IDHEM
InChIInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+2/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
InChIKeyKABFMIBPWCXCRK-RGGAHWMASA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1c2n3c(c1CCC(=O)O)C=C4C(=C(C5=[N]4[Fe]36[N]7=C(C=C8N6C(=C5)C(=C8C)C=C)C(=C(C7=C2)C)C=C)C)CCC(=O)O
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Fe]5|6|N2=C1C=c7n5c(=CC8=N|6C(=Cc4c(C)c3CCC(O)=O)C(=C8C=C)C)c(C)c7C=C
ACDLabs 12.01C=1c3c(c(c4C=C5C(=C(C=6C=C7C(=C(C8=CC=2C(=C(C=1N=2[Fe](n34)(N5=6)N78)CCC(=O)O)C)\C=C)C)\C=C)C)C)CCC(=O)O
FormulaC34 H32 Fe N4 O4
NamePROTOPORPHYRIN IX CONTAINING FE;
HEME
ChEMBL
DrugBankDB18267
ZINC
PDB chain6t0j Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6t0j Hydroxylation of Antitubercular Drug Candidate, SQ109, by Mycobacterial Cytochrome P450.
Resolution1.25 Å
Binding residue
(original residue number in PDB)		I111 H118 R122 A267 G268 T271 T272 P314 R320 G370 F371 H377 C379 L380 G381 A385
Binding residue
(residue number reindexed from 1)		I112 H119 R123 A268 G269 T272 T273 P315 R321 G371 F372 H378 C380 L381 G382 A386
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G199 A267 E270 T271 T272 C379 L380 G381 E388 I417
Catalytic site (residue number reindexed from 1) G200 A268 E271 T272 T273 C380 L381 G382 E389 I418
Enzyme Commision number 1.14.15.14: methyl-branched lipid omega-hydroxylase.
1.14.15.28: cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming].
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0008395 steroid hydroxylase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0031073 cholesterol 26-hydroxylase activity
GO:0036199 cholest-4-en-3-one 26-monooxygenase activity
GO:0046872 metal ion binding
GO:0070402 NADPH binding
Biological Process
GO:0006631 fatty acid metabolic process
GO:0006707 cholesterol catabolic process
GO:0010430 fatty acid omega-oxidation
GO:0097089 methyl-branched fatty acid metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6t0j, PDBe:6t0j, PDBj:6t0j
PDBsum6t0j
PubMed33081390
UniProtP9WPP3|CP124_MYCTU Methyl-branched lipid omega-hydroxylase (Gene Name=cyp124)

[Back to BioLiP]