Structure of PDB 2krj Chain A Binding Site BS01

Receptor Information
>2krj Chain A (length=152) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILV
VFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHSGGTN
LFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSL
YG
Ligand information
Ligand IDCO
InChIInChI=1S/Co/q+2
InChIKeyXLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Co+2]
CACTVS 3.341[Co++]
FormulaCo
NameCOBALT (II) ION
ChEMBL
DrugBankDB14205
ZINC
PDB chain2krj Chain A Residue 264 [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]
PDB2krj High-resolution solid-state NMR structure of a 17.6 kDa protein.
ResolutionN/A
Binding residue
(original residue number in PDB)		H218 H222 H228
Binding residue
(residue number reindexed from 1)		H107 H111 H117
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) H218 E219 H222 H228
Catalytic site (residue number reindexed from 1) H107 E108 H111 H117
Enzyme Commision number 3.4.24.65: macrophage elastase.
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0031012 extracellular matrix

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2krj, PDBe:2krj, PDBj:2krj
PDBsum2krj
PubMed20041641
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

[Back to BioLiP]