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3G5R

Crystal structure of Thermus thermophilus TrmFO in complex with tetrahydrofolate

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 Residues32
DetailsBINDING SITE FOR RESIDUE FAD A 444
ChainResidue
AGLY8
ASER52
AGLU119
AGLU120
AVAL121
AALA132
ATHR133
AGLY134
APRO135
ASER138
AGLY335
AGLY10
AVAL336
AGLY342
ATYR343
ASER346
ATHG445
AHOH453
AHOH460
AHOH461
AHOH466
AHOH476
ALEU11
AHOH480
AHOH522
AHOH557
AALA12
AGLU31
AMET32
AARG33
AHIS41
ACYS51

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE THG A 445
ChainResidue
APRO135
AHIS308
AARG309
AASN310
AFAD444
AHOH612
AHOH812
AHOH813

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 446
ChainResidue
ALEU84
AHOH512
AHOH556
AHOH739
AHOH740

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 447
ChainResidue
AHIS152
APHE153
AASN314
APHE390
AHOH567
AHOH679

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 448
ChainResidue
AILE301
AVAL302
ATYR304
ATYR394
AASN396
AHOH507
AHOH620

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 449
ChainResidue
ALYS360
AGLY363
APRO365
AHOH539
AHOH677

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 450
ChainResidue
APHE325
AARG326
AGLU329

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 451
ChainResidue
ALYS35
AMET37
APHE175
AARG176

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 452
ChainResidue
AGLU265
ATHR384
AALA385
AASN386
AHOH810

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 2024-07-24

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