Structure of PDB 2dfi Chain A Binding Site BS02
Receptor Information
>2dfi Chain A (length=301) Species:
2261
(Pyrococcus furiosus) [
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MDTEKLMKAGEIAKKVREKAIKLARPGMLLLELAESIEKMIMELGGKPAF
PVNLSINEIAAHYTPYKGDTTVLKEGDYLKIDVGVHIDGFIADTAVTVRV
GMEEDELMEAAKEALNAAISVARAGVEIKELGKAIENEIRKRGFKPIVNL
SGHKIERYKLHAGISIPNIYRPHDNYVLKEGDVFAIEPFATIGAGQVIEV
PPTLIYMYVRDVPVRVAQARFLLAKIKREYGTLPFAYRWLQNDMPEGQLK
LALKTLEKAGAIYGYPVLKEIRNGIVAQFEHTIIVEKDSVIVTQDMINKS
T
Ligand information
Ligand ID
CO
InChI
InChI=1S/Co/q+2
InChIKey
XLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Co+2]
CACTVS 3.341
[Co++]
Formula
Co
Name
COBALT (II) ION
ChEMBL
DrugBank
DB14205
ZINC
PDB chain
2dfi Chain A Residue 505 [
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Receptor-Ligand Complex Structure
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PDB
2dfi
Conformational contagion in a protein: Structural properties of a chameleon sequence
Resolution
2.1 Å
Binding residue
(original residue number in PDB)
D93 H153 E187 E280
Binding residue
(residue number reindexed from 1)
D93 H153 E187 E280
Annotation score
3
Enzymatic activity
Catalytic site (original residue number in PDB)
D82 D93 H153 H161 E187 E280
Catalytic site (residue number reindexed from 1)
D82 D93 H153 H161 E187 E280
Enzyme Commision number
3.4.11.18
: methionyl aminopeptidase.
Gene Ontology
Molecular Function
GO:0004177
aminopeptidase activity
GO:0004239
initiator methionyl aminopeptidase activity
GO:0008235
metalloexopeptidase activity
GO:0046872
metal ion binding
GO:0070006
metalloaminopeptidase activity
Biological Process
GO:0006508
proteolysis
Cellular Component
GO:0005737
cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:2dfi
,
PDBe:2dfi
,
PDBj:2dfi
PDBsum
2dfi
PubMed
17510955
UniProt
P56218
|MAP2_PYRFU Methionine aminopeptidase (Gene Name=map)
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