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5MVF

Active structure of EHD4 complexed with ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005769cellular_componentearly endosome
A0005783cellular_componentendoplasmic reticulum
A0005886cellular_componentplasma membrane
A0006897biological_processendocytosis
A0006907biological_processpinocytosis
A0030100biological_processregulation of endocytosis
A0030139cellular_componentendocytic vesicle
A0031901cellular_componentearly endosome membrane
A0032456biological_processendocytic recycling
A0046872molecular_functionmetal ion binding
A0048471cellular_componentperinuclear region of cytoplasm
A0050731biological_processpositive regulation of peptidyl-tyrosine phosphorylation
A0051260biological_processprotein homooligomerization
A0055038cellular_componentrecycling endosome membrane
A0060271biological_processcilium assembly
A0071363biological_processcellular response to growth factor stimulus
A0072659biological_processprotein localization to plasma membrane
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue ADP A 601
ChainResidue
ATYR70
ALYS223
AGLN226
ASER259
ATRP261
AMG602
ASER71
ATHR72
AGLY73
ALYS74
ATHR75
ATHR76
AILE91
AASN222

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 602
ChainResidue
ATHR75
AASP156
AADP601

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DCDCDGMLDeeEF
ChainResidueDetails
AASP492-PHE504

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8BH64
ChainResidueDetails
AGLY68
ALYS223
ATRP261

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
AASP492
AASP494
AASP496
AMET498
AGLU503

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9H223
ChainResidueDetails
ASER162

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9H223
ChainResidueDetails
ATYR451

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER459

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PDB entries from 2024-07-10

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