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6F87

Crystal structure of P. abyssi Sua5 complexed with L-threonine and PPi

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0002949biological_processtRNA threonylcarbamoyladenosine modification
A0003725molecular_functiondouble-stranded RNA binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0008033biological_processtRNA processing
A0016779molecular_functionnucleotidyltransferase activity
A0061710molecular_functionL-threonylcarbamoyladenylate synthase
B0000049molecular_functiontRNA binding
B0002949biological_processtRNA threonylcarbamoyladenosine modification
B0003725molecular_functiondouble-stranded RNA binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0008033biological_processtRNA processing
B0016779molecular_functionnucleotidyltransferase activity
B0061710molecular_functionL-threonylcarbamoyladenylate synthase
C0000049molecular_functiontRNA binding
C0002949biological_processtRNA threonylcarbamoyladenosine modification
C0003725molecular_functiondouble-stranded RNA binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0008033biological_processtRNA processing
C0016779molecular_functionnucleotidyltransferase activity
C0061710molecular_functionL-threonylcarbamoyladenylate synthase
D0000049molecular_functiontRNA binding
D0002949biological_processtRNA threonylcarbamoyladenosine modification
D0003725molecular_functiondouble-stranded RNA binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0008033biological_processtRNA processing
D0016779molecular_functionnucleotidyltransferase activity
D0061710molecular_functionL-threonylcarbamoyladenylate synthase
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue POP A 401
ChainResidue
ALYS56
AHIS234
AHOH504
AHOH511
AHOH514
AHOH518
AARG58
AASN62
ASER143
AASN145
ASER147
AGLY148
APRO228
AGLY229

site_idAC2
Number of Residues10
Detailsbinding site for residue THR A 402
ChainResidue
ATHR35
AVAL36
AGLY38
AILE65
AHIS67
AARG121
AALA141
AGLU180
ASER181
AARG195

site_idAC3
Number of Residues10
Detailsbinding site for residue POP B 401
ChainResidue
BLYS56
BARG58
BASN62
BSER143
BASN145
BSER147
BGLY148
BPRO228
BGLY229
BHIS234

site_idAC4
Number of Residues11
Detailsbinding site for residue THR B 402
ChainResidue
BTHR35
BVAL36
BGLY38
BILE65
BHIS67
BARG121
BALA141
BGLU180
BSER181
BARG195
BHOH507

site_idAC5
Number of Residues13
Detailsbinding site for residue POP C 401
ChainResidue
CLYS56
CARG58
CASN62
CSER143
CASN145
CSER147
CGLY148
CPRO228
CGLY229
CHIS234
CHOH513
CHOH517
CHOH521

site_idAC6
Number of Residues9
Detailsbinding site for residue THR C 402
ChainResidue
CTHR35
CGLY38
CILE65
CHIS67
CARG121
CALA141
CGLU180
CSER181
CARG195

site_idAC7
Number of Residues13
Detailsbinding site for residue POP D 401
ChainResidue
DLYS56
DARG58
DASN62
DSER143
DASN145
DSER147
DGLY148
DPRO228
DGLY229
DHIS234
DHOH504
DHOH507
DHOH514

site_idAC8
Number of Residues9
Detailsbinding site for residue THR D 402
ChainResidue
DTHR35
DGLY38
DILE65
DHIS67
DARG121
DALA141
DGLU180
DSER181
DARG195

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATHR35
ASER181
AARG195
ATYR235
BTHR35
BARG58
BASN62
BHIS67
BTHR117
BARG121
BALA141
AARG58
BSER143
BSER151
BSER181
BARG195
BTYR235
CTHR35
CARG58
CASN62
CHIS67
CTHR117
AASN62
CARG121
CALA141
CSER143
CSER151
CSER181
CARG195
CTYR235
DTHR35
DARG58
DASN62
AHIS67
DHIS67
DTHR117
DARG121
DALA141
DSER143
DSER151
DSER181
DARG195
DTYR235
ATHR117
AARG121
AALA141
ASER143
ASER151

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PDB entries from 2024-08-07

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