Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1EQR

CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003676molecular_functionnucleic acid binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004815molecular_functionaspartate-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006422biological_processaspartyl-tRNA aminoacylation
A0016874molecular_functionligase activity
A1901576biological_processorganic substance biosynthetic process
B0000166molecular_functionnucleotide binding
B0003676molecular_functionnucleic acid binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004815molecular_functionaspartate-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006422biological_processaspartyl-tRNA aminoacylation
B0016874molecular_functionligase activity
B1901576biological_processorganic substance biosynthetic process
C0000166molecular_functionnucleotide binding
C0003676molecular_functionnucleic acid binding
C0004812molecular_functionaminoacyl-tRNA ligase activity
C0004815molecular_functionaspartate-tRNA ligase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006412biological_processtranslation
C0006418biological_processtRNA aminoacylation for protein translation
C0006422biological_processaspartyl-tRNA aminoacylation
C0016874molecular_functionligase activity
C1901576biological_processorganic substance biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 901
ChainResidue
AGLU482
AHOH1042
AHOH1043
AHOH1046

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 902
ChainResidue
BGLU482
BHOH1030
BHOH1031

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 903
ChainResidue
CHOH1041
CHOH1042
CGLU482
CHOH1039

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00044
ChainResidueDetails
AGLU171
BGLN226
BHIS448
BGLU482
BARG489
BGLY534
CGLU171
CARG217
CGLN226
CHIS448
CGLU482
AARG217
CARG489
CGLY534
AGLN226
AHIS448
AGLU482
AARG489
AGLY534
BGLU171
BARG217

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon