Structure of PDB 1cmj Chain A Binding Site BS01

Receptor Information
>1cmj Chain A (length=399) Species: 5507 (Fusarium oxysporum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
APSFPFSRASGPEPPAEFAKLRATNPVSQVKLFDGSLAWLVTKHKDVCFV
ATSEKLSKVRTRQGFPELSASGKQAAKAKPTFVDMDPPEHMHQRSMVEPT
FTPEAVKNLQPYIQRTVDDLLEQMKQKGCANGPVDLVKEFALPVPSYIIY
TLLGVPFNDLEYLTQQNAIRTNGSSTAREASAANQELLDYLAILVEQRLV
EPKDDIISKLCTEQVKPGNIDKSDAVQIAFLLLVAGNATMVNMIALGVAT
LAQHPDQLAQLKANPSLAPQFVEELCRYHTATALAIKRTAKEDVMIGDKL
VRANEGIIASNQSANRDEEVFENPDEFNMNRKWPPQDPLGFGFGDHRCIA
EHLAKAELTTVFSTLYQKFPDLKVAVPLGKINYTPLNRDVGIVDLPVIF
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 chain1cmj 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

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PDB1cmj Proton delivery in NO reduction by fungal nitric-oxide reductase. Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		F86 V87 H94 R98 L236 A239 G240 T243 M244 G344 F345 G346 F347 H350 C352 I353 A354
Binding residue
(residue number reindexed from 1)		F82 V83 H90 R94 L232 A235 G236 T239 M240 G340 F341 G342 F343 H346 C348 I349 A350
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) T175 A239 A242 T243 M244 T286 C352 I353 A354 E361 D393
Catalytic site (residue number reindexed from 1) T171 A235 A238 T239 M240 T282 C348 I349 A350 E357 D389
Enzyme Commision number 1.7.1.14: nitric oxide reductase [NAD(P)(+), nitrous oxide-forming].
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
GO:0102199 nitric oxide reductase (NAD(P)H) activity

View graph for
Molecular Function
External links
PDB RCSB:1cmj, PDBe:1cmj, PDBj:1cmj
PDBsum1cmj
PubMed10671516
UniProtP23295|NOR_FUSOX NADP nitrous oxide-forming nitric oxide reductase (Gene Name=CYP55A1)

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