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6NBJ

Qri7

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0002949biological_processtRNA threonylcarbamoyladenosine modification
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006400biological_processtRNA modification
A0008033biological_processtRNA processing
A0008252molecular_functionnucleotidase activity
A0008270molecular_functionzinc ion binding
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0046872molecular_functionmetal ion binding
A0061711molecular_functiontRNA N(6)-L-threonylcarbamoyladenine synthase activity
A0070525biological_processtRNA threonylcarbamoyladenosine metabolic process
A0072670biological_processmitochondrial tRNA threonylcarbamoyladenosine modification
B0000049molecular_functiontRNA binding
B0002949biological_processtRNA threonylcarbamoyladenosine modification
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006400biological_processtRNA modification
B0008033biological_processtRNA processing
B0008252molecular_functionnucleotidase activity
B0008270molecular_functionzinc ion binding
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0046872molecular_functionmetal ion binding
B0061711molecular_functiontRNA N(6)-L-threonylcarbamoyladenine synthase activity
B0070525biological_processtRNA threonylcarbamoyladenosine metabolic process
B0072670biological_processmitochondrial tRNA threonylcarbamoyladenosine modification
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue ZN A 501
ChainResidue
AHIS145
AHIS149
AHIS175
AASP361
AHOH601
AHOH604

site_idAC2
Number of Residues13
Detailsbinding site for residue AMP A 502
ChainResidue
AASP203
AALA217
AARG218
AGLU221
AGLY324
AGLY325
ASER328
AASN329
AMET356
ASER360
ASER172
AGLY173
AGLY199

site_idAC3
Number of Residues5
Detailsbinding site for residue PGE A 503
ChainResidue
ALYS31
ATYR33
ALYS55
ATRP374
AARG378

site_idAC4
Number of Residues10
Detailsbinding site for residue ATP A 504
ChainResidue
AARG389
BLYS81
BHIS83
BMET118
BPRO119
BGLY120
BSER121
BSER246
BLYS308
CC3

site_idAC5
Number of Residues6
Detailsbinding site for residue ZN B 501
ChainResidue
BHIS145
BHIS149
BHIS175
BASP361
BHOH602
BHOH605

site_idAC6
Number of Residues12
Detailsbinding site for residue AMP B 502
ChainResidue
BSER172
BGLY173
BASP203
BALA217
BARG218
BGLU221
BGLY325
BVAL326
BSER328
BASN329
BSER360
BHOH602

site_idAC7
Number of Residues2
Detailsbinding site for residue SO4 B 503
ChainResidue
BLYS204
BARG265

Functional Information from PROSITE/UniProt
site_idPS01016
Number of Residues21
DetailsGLYCOPROTEASE Glycoprotease family signature. KGlavaWNkPlIgvhHmlGHL
ChainResidueDetails
ALYS130-LEU150

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03179","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23620299","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03179","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25084372","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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