Structure of PDB 6iw7 Chain N

Receptor sequence
>6iw7N (length=176) Species: 83331 (Mycobacterium tuberculosis CDC1551) [Search protein sequence]
LTDSVYERLLSERIIFLGSEVNDEIANRLCAQILLLAAEDASKDISLYIN
SPGGSISAGMAIYDTMVLAPCDIATYAMGMAASMGEFLLAAGTKGKRYAL
PHARILMHQPLGGVTGSAADIAIQAEQFAVIKKEMFRLNAEFTGQPIERI
EADSDRDRWFTAAEALEYGFVDHIIT
3D structure
PDB6iw7 structural insights into Mycobacterium tuberculosis ClpP1P2 inhibition by Cediranib: implications for developing antimicrobial agents targeting Clp protease
ChainN
Resolution2.69212 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G69 S98 M99 H123 D172
Catalytic site (residue number reindexed from 1) G54 S83 M84 H108 D157
Enzyme Commision number 3.4.21.92: endopeptidase Clp.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 AV3 N I71 S72 M75 I146 I56 S57 M60 I131
BS02 AV3 N G94 M95 H117 R119 W174 G79 M80 H102 R104 W159
BS03 S0R N S70 I71 P125 L126 S55 I56 P110 L111
BS04 LEU N G69 S98 M99 H123 G54 S83 M84 H108
Gene Ontology
Molecular Function
GO:0004176 ATP-dependent peptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0051117 ATPase binding
Biological Process
GO:0006508 proteolysis
GO:0006515 protein quality control for misfolded or incompletely synthesized proteins
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009368 endopeptidase Clp complex

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Molecular Function
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Cellular Component
External links
PDB RCSB:6iw7, PDBe:6iw7, PDBj:6iw7
PDBsum6iw7
PubMed
UniProtP9WPC5|CLPP1_MYCTU ATP-dependent Clp protease proteolytic subunit 1 (Gene Name=clpP1)

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