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6XRS

Crystal structure of a GTP-binding protein EngA (Der homolog) from Neisseria gonorrhoeae bound to GDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000027biological_processribosomal large subunit assembly
A0005525molecular_functionGTP binding
A0016887molecular_functionATP hydrolysis activity
A0042254biological_processribosome biogenesis
A0043022molecular_functionribosome binding
B0000027biological_processribosomal large subunit assembly
B0005525molecular_functionGTP binding
B0016887molecular_functionATP hydrolysis activity
B0042254biological_processribosome biogenesis
B0043022molecular_functionribosome binding
C0000027biological_processribosomal large subunit assembly
C0005525molecular_functionGTP binding
C0016887molecular_functionATP hydrolysis activity
C0042254biological_processribosome biogenesis
C0043022molecular_functionribosome binding
D0000027biological_processribosomal large subunit assembly
D0005525molecular_functionGTP binding
D0016887molecular_functionATP hydrolysis activity
D0042254biological_processribosome biogenesis
D0043022molecular_functionribosome binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue GDP A 601
ChainResidue
AASN200
ASER342
AALA343
ALEU344
AVAL201
AGLY202
ALYS203
ASER204
ATHR205
AASN309
ALYS310
AASP312

site_idAC2
Number of Residues12
Detailsbinding site for residue GDP B 601
ChainResidue
BASN200
BVAL201
BGLY202
BLYS203
BSER204
BTHR205
BASN309
BLYS310
BASP312
BSER342
BALA343
BLEU344

site_idAC3
Number of Residues25
Detailsbinding site for residue GDP B 602
ChainResidue
BASN27
BVAL28
BGLY29
BLYS30
BSER31
BTHR32
BARG108
BLYS135
BGLU137
BSER160
BGLY161
BALA162
BHOH703
BHOH705
BHOH706
BHOH718
DASN27
DVAL28
DGLY29
DLYS30
DSER31
DTHR32
DARG108
DLYS135
DALA162

site_idAC4
Number of Residues3
Detailsbinding site for residue CL B 604
ChainResidue
BGLY166
CARG215
CGLU234

site_idAC5
Number of Residues24
Detailsbinding site for residue GDP C 601
ChainResidue
AASN27
AVAL28
AGLY29
ALYS30
ASER31
ATHR32
AARG108
ALYS135
AGLU137
ASER160
AALA162
CASN27
CVAL28
CGLY29
CLYS30
CSER31
CTHR32
CASN134
CLYS135
CGLU137
CSER160
CGLY161
CALA162
CHOH703

site_idAC6
Number of Residues12
Detailsbinding site for residue GDP C 602
ChainResidue
CASN200
CVAL201
CGLY202
CLYS203
CSER204
CTHR205
CASN309
CLYS310
CASP312
CSER342
CALA343
CLEU344

site_idAC7
Number of Residues1
Detailsbinding site for residue CL C 604
ChainResidue
CLYS371

site_idAC8
Number of Residues2
Detailsbinding site for residue CL C 605
ChainResidue
CHIS59
CGLU271

site_idAC9
Number of Residues13
Detailsbinding site for residue GDP D 601
ChainResidue
DASP312
DSER342
DALA343
DLEU344
DHOH709
DASN200
DVAL201
DGLY202
DLYS203
DSER204
DTHR205
DASN309
DLYS310

site_idAD1
Number of Residues1
Detailsbinding site for residue IOD D 602
ChainResidue
DARG347

site_idAD2
Number of Residues2
Detailsbinding site for residue CL D 603
ChainResidue
DLYS17
DHIS59

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00195
ChainResidueDetails
AGLY24
BGLY197
BASP244
BASN309
CGLY24
CASP71
CASN134
CGLY197
CASP244
CASN309
DGLY24
AASP71
DASP71
DASN134
DGLY197
DASP244
DASN309
AASN134
AGLY197
AASP244
AASN309
BGLY24
BASP71
BASN134

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PDB entries from 2024-10-09

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