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3HXV

Crystal Structure of catalytic fragment of E. coli AlaRS in complex with GlySA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003676molecular_functionnucleic acid binding
A0004813molecular_functionalanine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006419biological_processalanyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE EPE A 442
ChainResidue
ASER25
AHOH915
AHOH931
AARG66
AGLU125
AARG152
AGLU346
AASP347
AHOH491
AHOH739
AHOH912

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE HED A 443
ChainResidue
AARG60
AASP100
ATYR101
APHE109
AARG396
AARG434
AHOH839
AHOH881
AHOH889

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE G5A A 444
ChainResidue
AALA41
AARG69
AASP76
AARG85
AHIS86
AHIS87
APHE90
AMET92
ATRP170
AGLU183
AGLU209
AILE210
AASN212
AASP235
AGLY237
AGLY239
AARG242
AHOH599
AHOH618
AHOH740
AHOH892

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BME A 445
ChainResidue
ASER1

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HED A 446
ChainResidue
APRO34
AARG305

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE HED A 447
ChainResidue
APHE120
ATYR186
AVAL246
ALEU247
AHIS249
AHOH544
AHOH584

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS73

218853

PDB entries from 2024-04-24

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