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3G5S

Crystal structure of Thermus thermophilus TrmFO in complex with glutathione

Functional Information from GO Data
ChainGOidnamespacecontents
A0002098biological_processtRNA wobble uridine modification
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008033biological_processtRNA processing
A0008168molecular_functionmethyltransferase activity
A0030488biological_processtRNA methylation
A0032259biological_processmethylation
A0047151molecular_functiontRNA (uracil(54)-C5)-methyltransferase activity, 5,10-methylenetetrahydrofolate-dependent
A0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues34
DetailsBINDING SITE FOR RESIDUE FAD A 444
ChainResidue
AGLY8
ACYS51
ASER52
AGLU119
AGLU120
AVAL121
AALA132
ATHR133
AGLY134
APRO135
ASER138
AGLY10
AHIS212
AGLY335
AVAL336
AGLU341
AGLY342
ATYR343
ASER346
AHOH642
AHOH644
AHOH658
ALEU11
AHOH659
AHOH665
AHOH682
AHOH696
AHOH752
AALA12
AGLU31
AMSE32
AARG33
ATHR38
AHIS41

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GSH A 445
ChainResidue
ATYR157
AASP158
AALA159
ASER161
ACYS223
ALEU274
AGLY276
AGLN278
ATYR312
AGLN391
AMG446
AEDO448
AHOH484
AHOH487
AHOH489
AHOH634
AHOH637

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 446
ChainResidue
AGLN391
AGSH445
AHOH634
AHOH635
AHOH636
AHOH637

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 447
ChainResidue
AGLU324
APHE325
AARG326
AGLU329
AHOH809

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 448
ChainResidue
AHIS152
APHE153
AASN314
APHE390
AGSH445
AHOH1087

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 449
ChainResidue
AGLU265
AASP266
ALYS267
ATHR384
AALA385
AASN386

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 450
ChainResidue
ALEU165
AGLU300
ATRP397
AARG413

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 451
ChainResidue
ALEU23
AGLY24
APHE239
ALYS243
ALEU362
AHOH578
AHOH938

Functional Information from PROSITE/UniProt
site_idPS01281
Number of Residues24
DetailsGIDA_2 Glucose inhibited division protein A family signature 2. AGVlAGveGYlESAATGFLAGLNA
ChainResidueDetails
AALA334-ALA357

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01037
ChainResidueDetails
AGLY8

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PDB entries from 2024-10-30

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