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3HY1

Crystal Structure of catalytic fragment of E. coli AlaRS G237A in complex with SerSA

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
B0000166molecular_functionnucleotide binding
B0003676molecular_functionnucleic acid binding
B0004813molecular_functionalanine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006419biological_processalanyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE SSA A 442
ChainResidue
AARG69
AILE210
AASN212
AASP235
AALA237
AGLY239
AARG242
AMG445
AHOH470
AASP76
AARG85
AHIS86
AHIS87
APHE90
AMET92
ATRP170
AGLU209

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HED A 443
ChainResidue
ATYR398
AASP399
AHOH453

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 444
ChainResidue
AARG85
AHIS86
AGLU209
AARG242
AMG445

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 445
ChainResidue
AGLU209
ASSA442
ASO4444

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MES B 442
ChainResidue
BVAL29
BHIS31
BARG60
BASP105
BASP296
BGLY297

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS73
BLYS73

222415

PDB entries from 2024-07-10

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