Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6F8Y

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0002949biological_processtRNA threonylcarbamoyladenosine modification
A0003725molecular_functiondouble-stranded RNA binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006450biological_processregulation of translational fidelity
A0008033biological_processtRNA processing
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0061710molecular_functionL-threonylcarbamoyladenylate synthase
B0000049molecular_functiontRNA binding
B0000166molecular_functionnucleotide binding
B0002949biological_processtRNA threonylcarbamoyladenosine modification
B0003725molecular_functiondouble-stranded RNA binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006450biological_processregulation of translational fidelity
B0008033biological_processtRNA processing
B0016740molecular_functiontransferase activity
B0016779molecular_functionnucleotidyltransferase activity
B0061710molecular_functionL-threonylcarbamoyladenylate synthase
C0000049molecular_functiontRNA binding
C0000166molecular_functionnucleotide binding
C0002949biological_processtRNA threonylcarbamoyladenosine modification
C0003725molecular_functiondouble-stranded RNA binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006450biological_processregulation of translational fidelity
C0008033biological_processtRNA processing
C0016740molecular_functiontransferase activity
C0016779molecular_functionnucleotidyltransferase activity
C0061710molecular_functionL-threonylcarbamoyladenylate synthase
D0000049molecular_functiontRNA binding
D0000166molecular_functionnucleotide binding
D0002949biological_processtRNA threonylcarbamoyladenosine modification
D0003725molecular_functiondouble-stranded RNA binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006450biological_processregulation of translational fidelity
D0008033biological_processtRNA processing
D0016740molecular_functiontransferase activity
D0016779molecular_functionnucleotidyltransferase activity
D0061710molecular_functionL-threonylcarbamoyladenylate synthase
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue THR A 401
ChainResidue
ATHR35
AGLY38
AILE65
AHIS67
AARG121
AALA141
AGLU180
ASER181
AARG195

site_idAC2
Number of Residues10
Detailsbinding site for residue THR B 401
ChainResidue
BTHR33
BTHR35
BVAL36
BGLY38
BHIS67
BARG121
BALA141
BGLU180
BSER181
BARG195

site_idAC3
Number of Residues9
Detailsbinding site for residue THR C 401
ChainResidue
CTHR35
CGLY38
CILE65
CHIS67
CARG121
CALA141
CGLU180
CSER181
CARG195

site_idAC4
Number of Residues10
Detailsbinding site for residue THR D 401
ChainResidue
DTHR35
DVAL36
DGLY38
DILE65
DHIS67
DARG121
DALA141
DGLU180
DSER181
DARG195

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues744
DetailsDomain: {"description":"YrdC-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00518","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues48
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

PDB statisticsPDBj update infoContact PDBjnumon