Structure of PDB 5mtv Chain A

Receptor sequence
>5mtvA (length=379) Species: 10090 (Mus musculus) [Search protein sequence]
GGSQTVTGGLRSLYQRKVLPLEEAYRFHEFHSPALEDADFENKPMILLVG
QYSTGKTTFIRYLLEQDFPGMRIGPEPTTDSFIAVMYGETEGSTPGNALV
VDPKKPFRKLSRFGNAFLNRFMCSQLPNQVLKSISIIDSPGILISRGYDF
CQVLQWFAERVDRIILLFDAHKLDISDEFSEAIKAFRGQDDKIRVVLNKA
DQVDTQQLMRVYGALMWSLGKVINTPEVLRVYIGSFWAQPLQNTDNRRLF
EAEAQDLFRDIQSLPQKAAVRKLNDLIKRARLAKVHAYIISYLKKEMPNM
FGKENKKRELIYRLPEIYVQLQREYQISAGDFPEVKAMQEQLENYDFTKF
HSLKPKLIEAVDNMLTNKISSLMGLISQE
3D structure
PDB5mtv Structural insights into the activation mechanism of dynamin-like EHD ATPases.
ChainA
Resolution2.79 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 AGS A S71 G73 K74 T75 T76 P93 D98 D156 K223 W261 S53 G55 K56 T57 T58 P75 D80 D138 K199 W237 PDBbind-CN: -logKd/Ki=4.11,Kd=77uM
BS02 MG A K74 T75 D156 K56 T57 D138
Gene Ontology
Molecular Function
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0005525 GTP binding
GO:0046872 metal ion binding
Biological Process
GO:0006907 pinocytosis
GO:0030100 regulation of endocytosis
GO:0032456 endocytic recycling
GO:0050731 positive regulation of peptidyl-tyrosine phosphorylation
GO:0051260 protein homooligomerization
GO:0071363 cellular response to growth factor stimulus
Cellular Component
GO:0005737 cytoplasm
GO:0005768 endosome
GO:0005783 endoplasmic reticulum
GO:0005886 plasma membrane
GO:0031901 early endosome membrane
GO:0048471 perinuclear region of cytoplasm
GO:0055038 recycling endosome membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5mtv, PDBe:5mtv, PDBj:5mtv
PDBsum5mtv
PubMed28228524
UniProtQ9EQP2|EHD4_MOUSE EH domain-containing protein 4 (Gene Name=Ehd4)

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