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2IVN

Structure of UP1 protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000408cellular_componentEKC/KEOPS complex
A0002949biological_processtRNA threonylcarbamoyladenosine modification
A0003727molecular_functionsingle-stranded RNA binding
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0006400biological_processtRNA modification
A0008033biological_processtRNA processing
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0046872molecular_functionmetal ion binding
A0061711molecular_functionN(6)-L-threonylcarbamoyladenine synthase activity
A0070525biological_processtRNA threonylcarbamoyladenosine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A1326
ChainResidue
AVAL145
APHE146
AGLU148
ALYS177
ALYS181
AASP196
AHOH2112
AHOH2201

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ANP A1327
ChainResidue
AHIS107
ATYR127
ASER129
AGLY130
AGLY131
AASN132
AGLY155
AASP159
AGLY172
APRO173
AGLU176
AGLY253
AVAL254
AASN257
ATYR280
AARG284
AASP285
AMG1328
AHOH2171
AHOH2175
AHOH2202
AHOH2203
ATHR9

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A1328
ChainResidue
AHIS111
ASER129
AGLY252
AGLY253
AASP285
AANP1327

Functional Information from PROSITE/UniProt
site_idPS01016
Number of Residues21
DetailsGLYCOPROTEASE Glycoprotease family signature. RAlavkYRkPiVgvnHciAHV
ChainResidueDetails
AARG92-VAL112

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01446, ECO:0000269|PubMed:17766251
ChainResidueDetails
AHIS107
AHIS111
ATYR127
AASP285

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AASP159
AGLY172
AGLU176
AASN257

221716

PDB entries from 2024-06-26

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