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4KVA

GTPase domain of Septin 10 from Schistosoma mansoni in complex with GTP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0019003molecular_functionGDP binding
A0031105cellular_componentseptin complex
A0031982cellular_componentvesicle
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0046982molecular_functionprotein heterodimerization activity
A0051260biological_processprotein homooligomerization
B0000287molecular_functionmagnesium ion binding
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0019003molecular_functionGDP binding
B0031105cellular_componentseptin complex
B0031982cellular_componentvesicle
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0046982molecular_functionprotein heterodimerization activity
B0051260biological_processprotein homooligomerization
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE GTP A 500
ChainResidue
ATHR50
AASP186
AVAL237
AGLY238
AARG253
ATYR255
AMG501
AHOH617
AHOH630
AHOH664
AHOH672
AGLY51
AHOH691
BTHR157
BTHR187
BGLU192
AILE52
AGLY53
ALYS54
ASER55
ATHR56
AGLU100
ALYS184

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
ASER55
AGLU100
AGTP500
AHOH690
AHOH691

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE GTP B 500
ChainResidue
ATHR187
AGLU192
BTHR50
BGLY51
BILE52
BGLY53
BLYS54
BSER55
BTHR56
BGLU100
BLYS184
BASP186
BVAL237
BGLY238
BARG253
BTYR255
BMG501
BHOH610
BHOH621
BHOH628
BHOH637

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 501
ChainResidue
BSER55
BGLU100
BGTP500
BHOH610
BHOH699

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:24464615, ECO:0007744|PDB:4KVA
ChainResidueDetails
AGLY51
BGLU100
BLYS184
BGLU192
BGLY238
BARG253
ASER55
AGLU100
ALYS184
AGLU192
AGLY238
AARG253
BGLY51
BSER55

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN405
BASN405

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PDB entries from 2024-11-06

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