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6H42

crystal structure of the human TGT catalytic subunit QTRT1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0006400biological_processtRNA modification
A0008033biological_processtRNA processing
A0008479molecular_functiontRNA-guanosine(34) queuine transglycosylase activity
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0032991cellular_componentprotein-containing complex
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0046982molecular_functionprotein heterodimerization activity
A0101030biological_processtRNA-guanine transglycosylation
A0120507cellular_componenttRNA-guanine transglycosylase complex
A1990234cellular_componenttransferase complex
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005741cellular_componentmitochondrial outer membrane
B0006400biological_processtRNA modification
B0008033biological_processtRNA processing
B0008479molecular_functiontRNA-guanosine(34) queuine transglycosylase activity
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0032991cellular_componentprotein-containing complex
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0046982molecular_functionprotein heterodimerization activity
B0101030biological_processtRNA-guanine transglycosylation
B0120507cellular_componenttRNA-guanine transglycosylase complex
B1990234cellular_componenttransferase complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue K A 501
ChainResidue
ATYR75
ALEU77
AARG80
AGLY82
AGLU84

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 502
ChainResidue
ACYS317
ACYS319
ACYS322
AHIS348

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 503
ChainResidue
ACYS23
ALYS367

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 505
ChainResidue
AVAL305
AHOH620

site_idAC5
Number of Residues4
Detailsbinding site for residue CL A 506
ChainResidue
APHE310
APHE310
ASER326
ASER326

site_idAC6
Number of Residues1
Detailsbinding site for residue CL A 507
ChainResidue
ACYS280

site_idAC7
Number of Residues5
Detailsbinding site for residue K B 501
ChainResidue
BTYR75
BLEU77
BARG80
BGLY82
BGLU84

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 502
ChainResidue
BCYS317
BCYS319
BCYS322
BHIS348

site_idAC9
Number of Residues1
Detailsbinding site for residue CL B 503
ChainResidue
AARG327

site_idAD1
Number of Residues4
Detailsbinding site for residue CL B 504
ChainResidue
BCYS23
BLYS367
BARG368
BPHE369

site_idAD2
Number of Residues1
Detailsbinding site for residue CL B 506
ChainResidue
BCYS280

site_idAD3
Number of Residues2
Detailsbinding site for residue CL B 507
ChainResidue
BPHE310
BSER326

site_idAD4
Number of Residues1
Detailsbinding site for residue BR B 508
ChainResidue
BGLU123

site_idAD5
Number of Residues2
Detailsbinding site for residue GLU B 509
ChainResidue
BARG184
BHOH601

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03218
ChainResidueDetails
AASP105
BASP105

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_03218
ChainResidueDetails
AASP279
BASP279

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:30149595, ECO:0000269|PubMed:34241577, ECO:0007744|PDB:6H45, ECO:0007744|PDB:7NQ4
ChainResidueDetails
AASP105
BGLY229
BCYS317
BCYS319
BCYS322
BHIS348
AASP159
AGLY229
ACYS317
ACYS319
ACYS322
AHIS348
BASP105
BASP159

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:34241577, ECO:0007744|PDB:7NQ4
ChainResidueDetails
AGLN202
BGLN202

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER139
BSER139

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PDB entries from 2024-07-17

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