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1E22

LYSYL-TRNA SYNTHETASE (LYSU) HEXAGONAL FORM complexed with lysine and the non-hydrolysable atp analogue amp-pcp

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003676molecular_functionnucleic acid binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004824molecular_functionlysine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006430biological_processlysyl-tRNA aminoacylation
A0016020cellular_componentmembrane
A0016874molecular_functionligase activity
A0034605biological_processcellular response to heat
A0036260biological_processRNA capping
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 515
ChainResidue
AARG412
AGLU414
AGLU421
AACP512
AMG517

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 516
ChainResidue
AGLU264
AACP512
AHOH2172
AHOH2303

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 517
ChainResidue
AGLU421
AACP512
AMG515

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE LYS A 510
ChainResidue
AGLY216
AALA217
AGLU240
AARG262
AMET276
AGLU278
ATYR280
AASN424
APHE426
AGLU428
AGLY473
AACP512
AGOL523

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE ACP A 512
ChainResidue
AARG262
AGLU264
AARG269
AHIS270
AASN271
APHE274
AGLU380
AGLU414
AGLU421
AILE422
AGLY477
AARG480
AILE491
ALYS510
AMG515
AMG516
AMG517
AGOL523
AHOH2258
AHOH2302
AHOH2303

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 520
ChainResidue
ATYR312
AHIS315
AILE384
AGLY418
AARG420
AHIS489

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 521
ChainResidue
AARG194
AARG194
AGLU204
AGLU206
AILE257
AASN258
AASN258
AHOH2169

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 522
ChainResidue
ATYR286
AGLU391
AASN403
ATHR410
AASP411
AARG412

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 523
ChainResidue
AALA217
ASER218
AVAL396
AARG412
AASN424
APHE426
ALYS510
AACP512
AHOH2152
AHOH2305

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOL A 524
ChainResidue
APRO214
AGLY215
AALA217
ASER218
AALA219
APRO221
AILE237
ALYS446
AGLU452
AALA453
AMET454
APHE455

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 525
ChainResidue
AVAL33
ALYS333
AARG402
AASN403
AASP404
AHOH2250
AHOH2306

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING:
ChainResidueDetails
APHE415
AILE422

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS114
APHE156

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1asy
ChainResidueDetails
AARG480
AGLU278
AARG262

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1asy
ChainResidueDetails
AARG262

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PDB entries from 2025-05-28

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