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1H3N

Leucyl-tRNA synthetase from Thermus thermophilus complexed with a sulphamoyl analogue of leucyl-adenylate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002161molecular_functionaminoacyl-tRNA editing activity
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004823molecular_functionleucine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006429biological_processleucyl-tRNA aminoacylation
A0046872molecular_functionmetal ion binding
A0106074biological_processaminoacyl-tRNA metabolism involved in translational fidelity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1817
ChainResidue
ACYS439
ACYS442
ACYS484
ACYS487

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1818
ChainResidue
ACYS159
ACYS162
ACYS176
AHIS179

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1819
ChainResidue
AGLU715
AGLY716
AARG719
ALYS760
ALEU714

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1820
ChainResidue
AGLY707
AARG769
ATRP795
AHOH2533
AHOH2534

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A1821
ChainResidue
ATHR247
ATHR248
ATYR332
AHOH2208

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LEU A1815
ChainResidue
APHE41
ATYR43
AASP80
ATYR535
AHIS541
AHIS545
ALMS1816
AHOH2366

site_idAC7
Number of Residues19
DetailsBINDING SITE FOR RESIDUE LMS A1816
ChainResidue
APRO42
ATYR43
AHIS49
AGLY51
AHIS52
AASN55
ATYR56
AGLY537
AGLY538
AGLU540
AGLN574
AMET576
AVAL577
AMET638
ALEU1815
AHOH2528
AHOH2530
AHOH2531
AHOH2532

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PypSGdLHMGHL
ChainResidueDetails
APRO42-LEU53

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a8h
ChainResidueDetails
AVAL637
ALYS640

222624

PDB entries from 2024-07-17

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