Structure of PDB 3oo5 Chain B Binding Site BS01

Receptor Information
>3oo5 Chain B (length=143) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLST
PDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDP
ENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAH
Ligand information
Ligand IDNTE
InChIInChI=1S/C34H33N5O6.Fe/c1-6-21-17(2)27-15-30-24(11-12-39(44)45)20(5)26(36-30)13-25-18(3)22(7-9-33(40)41)31(37-25)16-32-23(8-10-34(42)43)19(4)28(38-32)14-29(21)35-27;/h6,11-16H,1,7-10H2,2-5H3,(H4,35,36,37,38,40,41,42,43);/q;+2/p-2/b12-11+,25-13-,26-13-,27-15-,28-14-,29-14-,30-15-,31-16-,32-16-;
InChIKeyMBEUICWDKPMPCN-RXJYIKGQSA-L
SMILES
SoftwareSMILES
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Fe]5|6|N2=C1C=c7n5c(=CC8=N|6C(=Cc4c(C)c3CCC(O)=O)C(=C8\C=C\[N+]([O-])=O)C)c(C)c7C=C
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[N+]([O-])=O)C)c(C)c7C=C
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/[N+](=O)[O-])C)CCC(=O)O
ACDLabs 12.01N45[Fe]26n1c8c(c(c1C=C3N2=C(C(=C3C)\C=C\[N+]([O-])=O)C=C4C(=C(C5=CC7=N6C(C(=C7C)CCC(=O)O)=C8)\C=C)C)C)CCC(O)=O
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[N+](=O)[O-])C)CCC(=O)O
FormulaC34 H31 Fe N5 O6
Name[3,3'-{7-ethenyl-3,8,13,17-tetramethyl-12-[(E)-2-nitroethenyl]porphyrin-2,18-diyl-kappa~4~N~21~,N~22~,N~23~,N~24~}dipro panoato(2-)]iron;
Nitriheme
ChEMBL
DrugBank
ZINC
PDB chain3oo5 Chain B Residue 147 [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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PDB3oo5 Crystallographic Trapping of Heme Loss Intermediates during the Nitrite-Induced Degradation of Human Hemoglobin.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		F41 F42 H63 L88 H92 L96 V98 N102 F103 L106 V137 L141
Binding residue
(residue number reindexed from 1)		F41 F42 H63 L88 H92 L96 V98 N102 F103 L106 V137 L141
Annotation score1
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0005344 oxygen carrier activity
GO:0005515 protein binding
GO:0019825 oxygen binding
GO:0020037 heme binding
GO:0030492 hemoglobin binding
GO:0031720 haptoglobin binding
GO:0031721 hemoglobin alpha binding
GO:0043177 organic acid binding
GO:0046872 metal ion binding
Biological Process
GO:0008217 regulation of blood pressure
GO:0015670 carbon dioxide transport
GO:0015671 oxygen transport
GO:0030185 nitric oxide transport
GO:0042542 response to hydrogen peroxide
GO:0042744 hydrogen peroxide catabolic process
GO:0045429 positive regulation of nitric oxide biosynthetic process
GO:0070293 renal absorption
GO:0070527 platelet aggregation
GO:0097746 blood vessel diameter maintenance
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005829 cytosol
GO:0005833 hemoglobin complex
GO:0031838 haptoglobin-hemoglobin complex
GO:0070062 extracellular exosome
GO:0071682 endocytic vesicle lumen
GO:0072562 blood microparticle
GO:1904724 tertiary granule lumen
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3oo5, PDBe:3oo5, PDBj:3oo5
PDBsum3oo5
PubMed21863786
UniProtP68871|HBB_HUMAN Hemoglobin subunit beta (Gene Name=HBB)

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