5V58

Crystal structure of human prolyl-tRNA synthetase in complex with Aze-SA

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Functional Information from GO Data

ChainGOidnamespacecontents
A0017101cellular_componentaminoacyl-tRNA synthetase multienzyme complex
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0097452cellular_componentGAIT complex
A0016020cellular_componentmembrane
A0005886cellular_componentplasma membrane
A1990904cellular_componentribonucleoprotein complex
A0005524molecular_functionATP binding
A0004818molecular_functionglutamate-tRNA ligase activity
A0051020molecular_functionGTPase binding
A0042802molecular_functionidentical protein binding
A0004827molecular_functionproline-tRNA ligase activity
A0042803molecular_functionprotein homodimerization activity
A0035613molecular_functionRNA stem-loop binding
A0008270molecular_functionzinc ion binding
A0032869biological_processcellular response to insulin stimulus
A0071346biological_processcellular response to interferon-gamma
A0006424biological_processglutamyl-tRNA aminoacylation
A0044539biological_processlong-chain fatty acid import
A0017148biological_processnegative regulation of translation
A0006433biological_processprolyl-tRNA aminoacylation
A0065003biological_processprotein-containing complex assembly
A0006418biological_processtRNA aminoacylation for protein translation
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
AC116binding site for residue 8X1 A 1601
ChainResidue
ATHR1121
AGLU1123
AARG1152
AGLU1154
APHE1161
ALEU1162
ATHR1164
APHE1167
ATRP1169
AGLN1237
AGLY1239
ATHR1240
AHIS1242
AGLY1274
ATHR1276
AARG1278

AC25binding site for residue ZN A 1602
ChainResidue
ACYS1448
ACYS1453
ACYS1495
ACYS1497
AASN1500

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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
8X1_5v58_A_1601255'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine binding site
ChainResidueligand
APRO1120-THR11218X1: 5'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine
AGLU11238X1: 5'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine
AARG11528X1: 5'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine
AGLU11548X1: 5'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine
APHE1161-THR11648X1: 5'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine
APHE11678X1: 5'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine
ATRP11698X1: 5'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine
AGLU11718X1: 5'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine
AHIS11738X1: 5'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine
APHE12168X1: 5'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine
AGLN1237-THR12408X1: 5'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine
AHIS12428X1: 5'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine
ASER1272-THR12768X1: 5'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine
AARG12788X1: 5'-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine

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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
SWS_FT_FI13Zinc. {ECO:0000244|PDB:4HVC, ECO:0000244|PDB:4K86, ECO:0000244|PDB:4K87, ECO:0000244|PDB:4K88, ECO:0000269|PubMed:23263184, ECO:0000269|PubMed:24100331}
ChainResidueDetails
ACYS460
ACYS502
ACYS504

SWS_FT_FI21Zinc. {ECO:0000244|PDB:4HVC, ECO:0000244|PDB:4K86, ECO:0000244|PDB:4K87, ECO:0000269|PubMed:23263184, ECO:0000269|PubMed:24100331}
ChainResidueDetails
ACYS455

SWS_FT_FI31ATP. {ECO:0000244|PDB:4HVC, ECO:0000244|PDB:4K87, ECO:0000269|PubMed:23263184, ECO:0000269|PubMed:24100331}.
ChainResidueDetails
ATHR283

SWS_FT_FI42ATP. {ECO:0000250}.
ChainResidueDetails
ANA*
ANA*

SWS_FT_FI52L-proline. {ECO:0000244|PDB:4K87, ECO:0000269|PubMed:24100331}.
ChainResidueDetails
AARG159
AHIS249

SWS_FT_FI69ATP. {ECO:0000244|PDB:4HVC, ECO:0000244|PDB:4K87, ECO:0000269|PubMed:23263184, ECO:0000269|PubMed:24100331}.
ChainResidueDetails
AARG159-GLU161
AARG170-THR171
AGLN244-THR247

SWS_FT_FI75ATP. {ECO:0000250}.
ChainResidueDetails
ANA*

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Catalytic Information from CSA

site_idNumber of ResiduesDetails