Structure of PDB 4rom Chain C Binding Site BS02

Receptor Information
>4rom Chain C (length=141) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSH
GSAQVKGHGKKVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKL
LSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR
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 chain4rom Chain C Residue 201 [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]
PDB4rom Identification of a novel class of covalent modifiers of hemoglobin as potential antisickling agents.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		F43 H45 F46 H58 L83 L86 H87 L91 V93 N97 F98 L101 L136
Binding residue
(residue number reindexed from 1)		F43 H45 F46 H58 L83 L86 H87 L91 V93 N97 F98 L101 L136
Annotation score4
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0005344 oxygen carrier activity
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0019825 oxygen binding
GO:0020037 heme binding
GO:0031720 haptoglobin binding
GO:0043177 organic acid binding
GO:0046872 metal ion binding
Biological Process
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:0098869 cellular oxidant detoxification
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005829 cytosol
GO:0005833 hemoglobin complex
GO:0016020 membrane
GO:0031838 haptoglobin-hemoglobin complex
GO:0070062 extracellular exosome
GO:0071682 endocytic vesicle lumen
GO:0072562 blood microparticle

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4rom, PDBe:4rom, PDBj:4rom
PDBsum4rom
PubMed25974708
UniProtP69905|HBA_HUMAN Hemoglobin subunit alpha (Gene Name=HBA1)

[Back to BioLiP]