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2IVP

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 Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A1326
ChainResidue
AHIS107
AHIS111
ATYR127
AASP285
AATP1327

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP A1327
ChainResidue
AGLY130
AGLY131
AASN132
AGLY155
AASP159
AGLY172
AGLU176
AGLY253
AALA256
AASN257
ATYR280
AARG284
AASP285
AFE21326
ATHR9
AHIS107
ATYR127
ASER129

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

220760

PDB entries from 2024-06-05

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