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3HXU

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

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 Residues21
DetailsBINDING SITE FOR RESIDUE A5A A 442
ChainResidue
AALA41
AGLU209
AILE210
AASN212
AASP235
ATHR236
AGLY237
AGLY239
AARG242
AHOH496
AHOH568
AARG69
AHOH633
AHOH649
AASP76
AARG85
AHIS86
AHIS87
APHE90
AMET92
ATRP170

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HED A 443
ChainResidue
AARG60
AASP100
ATYR101
APHE109
AARG396
AARG434
AHOH616
AHOH627

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE EPE A 444
ChainResidue
ASER25
AARG66
ALYS124
AGLU125
AARG152
AGLU346
AASP347
AHOH510
AHOH847
AHOH1009
AHOH1013
AHOH1073

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BME A 445
ChainResidue
AARG305

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME A 446
ChainResidue
ATYR186
AHIS249

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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