Structure of PDB 2rgz Chain A Binding Site BS01

Receptor Information
>2rgz Chain A (length=214) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTY
SALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQAP
KAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLP
STGEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFE
YNMQIFNELDQAGS
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 chain2rgz Chain A Residue 300 [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]
PDB2rgz Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2.
Resolution2.61 Å
Binding residue
(original residue number in PDB)		H45 E49 V54 Y154 T155 M158 G159 S162 K199 R203 F227 N230
Binding residue
(residue number reindexed from 1)		H17 E21 V26 Y126 T127 M130 G131 S134 K171 R175 F199 N202
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) N50 Y78 T155 R156 G159 D160 G164
Catalytic site (residue number reindexed from 1) N22 Y50 T127 R128 G131 D132 G136
Enzyme Commision number 1.14.14.18: heme oxygenase (biliverdin-producing).
Gene Ontology
Molecular Function
GO:0004392 heme oxygenase (decyclizing) activity
Biological Process
GO:0006788 heme oxidation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2rgz, PDBe:2rgz, PDBj:2rgz
PDBsum2rgz
PubMed17965015
UniProtP30519|HMOX2_HUMAN Heme oxygenase 2 (Gene Name=HMOX2)

[Back to BioLiP]