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1NJ2

Crystal structure of Prolyl-tRNA Synthetase from Methanothermobacter thermautotrophicus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004827molecular_functionproline-tRNA ligase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006433biological_processprolyl-tRNA aminoacylation
A0016874molecular_functionligase activity
A0017101cellular_componentaminoacyl-tRNA synthetase multienzyme complex
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 495
ChainResidue
ACYS436
ACYS441
ACYS464
ACYS467

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 496
ChainResidue
AASP452

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:12578991
ChainResidueDetails
ATHR117
AGLU119
AARG148
AGLU150
AGLN232
ATHR235
AHIS237
ASER269

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12578991
ChainResidueDetails
ACYS436
ACYS441
ACYS464
ACYS467

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數據於2024-03-27公開中

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