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3X1D

Crystal Structure of Atlastin from Drosophila melanogaster

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0005874cellular_componentmicrotubule
A0007019biological_processmicrotubule depolymerization
A0007029biological_processendoplasmic reticulum organization
A0007030biological_processGolgi organization
A0007517biological_processmuscle organ development
A0007528biological_processneuromuscular junction development
A0008582biological_processregulation of synaptic assembly at neuromuscular junction
A0012505cellular_componentendomembrane system
A0016020cellular_componentmembrane
A0016320biological_processendoplasmic reticulum membrane fusion
A0016787molecular_functionhydrolase activity
A0030742molecular_functionGTP-dependent protein binding
A0031114biological_processregulation of microtubule depolymerization
A0032561molecular_functionguanyl ribonucleotide binding
A0042802molecular_functionidentical protein binding
A0048691biological_processpositive regulation of axon extension involved in regeneration
A0051124biological_processsynaptic assembly at neuromuscular junction
A0051260biological_processprotein homooligomerization
A0061025biological_processmembrane fusion
A0061709biological_processreticulophagy
A0140506molecular_functionendoplasmic reticulum-autophagosome adaptor activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GDP A 601
ChainResidue
APHE47
AHIS246
APRO247
AVAL251
AALA252
APHE268
AMG602
AARG48
ALYS49
AGLY50
ALYS51
ASER52
APHE53
AARG192
AASP193

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 602
ChainResidue
ALYS51
ASER52
ATHR122
AGDP601

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues494
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1-ALA424
AARG470-SER541

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AVAL425-LEU445
AALA449-ILE469

site_idSWS_FT_FI3
Number of Residues2
DetailsTOPO_DOM: Lumenal => ECO:0000255
ChainResidueDetails
ATYR446-PHE448

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY45
AARG93
AARG192
AVAL251

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:18327897
ChainResidueDetails
ATHR514

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PDB entries from 2024-10-16

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