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6ZQT

Crystal structure of the RLIP76 Ral binding domain mutant (E427H/Q433L/K440R) in complex with RalB-GMPPNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0001928biological_processregulation of exocyst assembly
A0001934biological_processpositive regulation of protein phosphorylation
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005886cellular_componentplasma membrane
A0006915biological_processapoptotic process
A0007165biological_processsignal transduction
A0007265biological_processRas protein signal transduction
A0009267biological_processcellular response to starvation
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019003molecular_functionGDP binding
A0030496cellular_componentmidbody
A0031623biological_processreceptor internalization
A0031625molecular_functionubiquitin protein ligase binding
A0032091biological_processnegative regulation of protein binding
A0032092biological_processpositive regulation of protein binding
A0045742biological_processpositive regulation of epidermal growth factor receptor signaling pathway
A0051117molecular_functionATPase binding
A0051301biological_processcell division
A0060178biological_processregulation of exocyst localization
A0070062cellular_componentextracellular exosome
A0071360biological_processcellular response to exogenous dsRNA
A0071902biological_processpositive regulation of protein serine/threonine kinase activity
A2000786biological_processpositive regulation of autophagosome assembly
B0001928biological_processregulation of exocyst assembly
B0001934biological_processpositive regulation of protein phosphorylation
B0003924molecular_functionGTPase activity
B0003925molecular_functionG protein activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005886cellular_componentplasma membrane
B0006915biological_processapoptotic process
B0007165biological_processsignal transduction
B0007265biological_processRas protein signal transduction
B0009267biological_processcellular response to starvation
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0019003molecular_functionGDP binding
B0030496cellular_componentmidbody
B0031623biological_processreceptor internalization
B0031625molecular_functionubiquitin protein ligase binding
B0032091biological_processnegative regulation of protein binding
B0032092biological_processpositive regulation of protein binding
B0045742biological_processpositive regulation of epidermal growth factor receptor signaling pathway
B0051117molecular_functionATPase binding
B0051301biological_processcell division
B0060178biological_processregulation of exocyst localization
B0070062cellular_componentextracellular exosome
B0071360biological_processcellular response to exogenous dsRNA
B0071902biological_processpositive regulation of protein serine/threonine kinase activity
B2000786biological_processpositive regulation of autophagosome assembly
C0005096molecular_functionGTPase activator activity
C0007264biological_processsmall GTPase-mediated signal transduction
C0031267molecular_functionsmall GTPase binding
D0005096molecular_functionGTPase activator activity
D0007264biological_processsmall GTPase-mediated signal transduction
D0031267molecular_functionsmall GTPase binding
Functional Information from PDB Data
site_idAC1
Number of Residues29
Detailsbinding site for residue GNP A 201
ChainResidue
AGLY23
AGLU41
AASP42
ATYR43
APRO45
ATHR46
AGLY71
AASN128
ALYS129
AASP131
ALEU132
AGLY24
ASER158
AALA159
ALYS160
AMG202
AHOH316
AHOH330
AHOH354
AHOH369
AHOH381
BARG162
AVAL25
AGLY26
ALYS27
ASER28
AALA29
APHE39
AVAL40

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 202
ChainResidue
ASER28
ATHR46
AGNP201
AHOH316
AHOH330

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL C 501
ChainResidue
AALA48
CGLU406
CARG440
CHOH622

site_idAC4
Number of Residues27
Detailsbinding site for residue GNP B 201
ChainResidue
BGLY23
BGLY24
BVAL25
BGLY26
BLYS27
BSER28
BALA29
BPHE39
BVAL40
BGLU41
BTYR43
BPRO45
BTHR46
BGLY71
BASN128
BLYS129
BASP131
BLEU132
BSER158
BALA159
BLYS160
BMG202
BHOH329
BHOH332
BHOH337
BHOH371
BHOH379

site_idAC5
Number of Residues5
Detailsbinding site for residue MG B 202
ChainResidue
BSER28
BTHR46
BGNP201
BHOH329
BHOH337

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:11300797
ChainResidueDetails
CGLY418
DGLY418
AASN128
ASER158
BGLY21
BASP68
BASN128
BSER158

227344

PDB entries from 2024-11-13

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