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2GIL

Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8 resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
D0003924molecular_functionGTPase activity
D0005525molecular_functionGTP binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1201
ChainResidue
ATHR27
ATHR45
AGTP1200
AHOH1304
AHOH1305

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 2201
ChainResidue
BHOH2336
BTHR27
BTHR45
BGTP2200
BHOH2335

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 3201
ChainResidue
CTHR27
CTHR45
CGTP3200
CHOH3331
CHOH3332

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 4201
ChainResidue
DTHR27
DTHR45
DGTP4200
DHOH4329
DHOH4330

site_idAC5
Number of Residues27
DetailsBINDING SITE FOR RESIDUE GTP A 1200
ChainResidue
AGLN22
ASER23
AVAL24
AGLY25
ALYS26
ATHR27
ASER28
APHE38
AASP39
AASN40
ATYR42
AALA44
ATHR45
AGLY71
AASN126
ALYS127
AASP129
ALEU130
ASER156
AALA157
ALYS158
AMG1201
AHOH1211
AHOH1222
AHOH1225
AHOH1304
AHOH1305

site_idAC6
Number of Residues30
DetailsBINDING SITE FOR RESIDUE GTP B 2200
ChainResidue
BGLN22
BSER23
BVAL24
BGLY25
BLYS26
BTHR27
BSER28
BPHE38
BASP39
BASN40
BTYR42
BTHR45
BGLY71
BASN126
BLYS127
BASP129
BLEU130
BSER156
BALA157
BLYS158
BMG2201
BHOH2203
BHOH2215
BHOH2233
BHOH2261
BHOH2303
BHOH2304
BHOH2335
BHOH2336
DTYR161

site_idAC7
Number of Residues29
DetailsBINDING SITE FOR RESIDUE GTP C 3200
ChainResidue
CHOH3207
CHOH3212
CHOH3222
CHOH3242
CHOH3243
CHOH3331
CHOH3332
CGLN22
CSER23
CVAL24
CGLY25
CLYS26
CTHR27
CSER28
CPHE38
CASP39
CASN40
CTYR42
CALA44
CTHR45
CGLY71
CASN126
CLYS127
CASP129
CLEU130
CSER156
CALA157
CLYS158
CMG3201

site_idAC8
Number of Residues29
DetailsBINDING SITE FOR RESIDUE GTP D 4200
ChainResidue
BTYR161
DGLN22
DSER23
DVAL24
DGLY25
DLYS26
DTHR27
DSER28
DPHE38
DASP39
DASN40
DTYR42
DTHR45
DGLY71
DASN126
DLYS127
DASP129
DLEU130
DSER156
DALA157
DLYS158
DMG4201
DHOH4205
DHOH4224
DHOH4229
DHOH4261
DHOH4329
DHOH4330
DHOH4334

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:16332443, ECO:0000269|PubMed:18243103, ECO:0000269|PubMed:19141279
ChainResidueDetails
AGLU21
ATHR69
ALYS127
AALA157
BGLU21
BTHR69
BLYS127
BALA157
CGLU21
CTHR69
CLYS127
CALA157
DGLU21
DTHR69
DLYS127
DALA157

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: O-AMP-tyrosine; by Legionella DrrA => ECO:0000269|PubMed:21822290
ChainResidueDetails
AILE83
DILE83
BILE83
CILE83

219869

PDB entries from 2024-05-15

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