Structure of PDB 1tg6 Chain G Binding Site BS01
Receptor Information
>1tg6 Chain G (length=194) Species:
9606
(Homo sapiens) [
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PLIPIVVYDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKKPI
HMYINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAASMGSLLLAAGTPG
MRHSLPNSRIMIHQPSGGARGQATDIAIQAEEIMKLKKQLYNIYAKHTKQ
SLQVIESAMERDRYMSPMEAQEFGILDKVLVHPPQDGEDEPTLV
Ligand information
Ligand ID
FME
InChI
InChI=1S/C6H11NO3S/c1-11-3-2-5(6(9)10)7-4-8/h4-5H,2-3H2,1H3,(H,7,8)(H,9,10)/t5-/m0/s1
InChIKey
PYUSHNKNPOHWEZ-YFKPBYRVSA-N
SMILES
Software
SMILES
CACTVS 3.341
CSCC[C@H](NC=O)C(O)=O
CACTVS 3.341
CSCC[CH](NC=O)C(O)=O
ACDLabs 10.04
O=CNC(C(=O)O)CCSC
OpenEye OEToolkits 1.5.0
CSCCC(C(=O)O)NC=O
OpenEye OEToolkits 1.5.0
CSCC[C@@H](C(=O)O)NC=O
Formula
C6 H11 N O3 S
Name
N-FORMYLMETHIONINE
ChEMBL
DrugBank
DB04464
ZINC
ZINC000001529464
PDB chain
1tg6 Chain D Residue 1106 [
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Receptor-Ligand Complex Structure
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PDB
1tg6
Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP
Resolution
2.1 Å
Binding residue
(original residue number in PDB)
G67 G68 V70 S97 M98 H122 P124
Binding residue
(residue number reindexed from 1)
G58 G59 V61 S88 M89 H113 P115
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
G68 S97 M98 H122 D171
Catalytic site (residue number reindexed from 1)
G59 S88 M89 H113 D162
Enzyme Commision number
3.4.21.92
: endopeptidase Clp.
Gene Ontology
Molecular Function
GO:0004175
endopeptidase activity
GO:0004176
ATP-dependent peptidase activity
GO:0004252
serine-type endopeptidase activity
GO:0005515
protein binding
GO:0008233
peptidase activity
GO:0008236
serine-type peptidase activity
GO:0042802
identical protein binding
GO:0051117
ATPase binding
Biological Process
GO:0006508
proteolysis
GO:0006515
protein quality control for misfolded or incompletely synthesized proteins
GO:0033619
membrane protein proteolysis
GO:0035694
mitochondrial protein catabolic process
GO:0051603
proteolysis involved in protein catabolic process
Cellular Component
GO:0005739
mitochondrion
GO:0005759
mitochondrial matrix
GO:0009368
endopeptidase Clp complex
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1tg6
,
PDBe:1tg6
,
PDBj:1tg6
PDBsum
1tg6
PubMed
15522782
UniProt
Q16740
|CLPP_HUMAN ATP-dependent Clp protease proteolytic subunit, mitochondrial (Gene Name=CLPP)
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