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UniProt G0SCK6

Ribosome biogenesis protein ERB1 (G0SCK6)

Ribosome biogenesis protein ERB1 (UniProt G0SCK6): 12 experimental structures and 1 predicted model on GenesisL1, 1 ligand bound, 17 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
G0SCK6
Protein
Ribosome biogenesis protein ERB1
Experimental structures
12
Predicted models
1
Ligands
1
Pockets
17 · 7 records with a druggable one

Structures

13 records of G0SCK6 in the MolNFT archive: 12 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
5CXBStructure of YTM1 bound to the C-terminal domain of ERB1 in P21 21 2 space groupx-ray diffractionB——
5CXCStructure of YTM1 bound to the C-terminal domain of ERB1 in P 65 2 2 space groupx-ray diffractionB——
5CYKStructure of YTM1 bound to the C-terminal domain of ERB1-R486Ex-ray diffractionB——
5EM2Crystal structure of the Erb1-Ytm1 complexx-ray diffractionA, CMG—
5EM2Crystal structure of the ERB1-YTM1 complexx-ray diffractionA, C——
8I9PCryo-EM structure of a Chaetomium thermophilum pre-60S ribosomal subunit - State Mak16electron microscopyCC—1 (best 0.88)
8I9TCryo-EM structure of a Chaetomium thermophilum pre-60S ribosomal subunit - State Dbp10-1electron microscopyCC—2 (best 0.89)
8I9VCryo-EM structure of a Chaetomium thermophilum pre-60S ribosomal subunit - State Dbp10-2electron microscopyCC—1 (best 0.87)
8I9XCryo-EM structure of a Chaetomium thermophilum pre-60S ribosomal subunit - Ytm1-1electron microscopyCC—3 (best 0.88)
8I9YCryo-EM structure of a Chaetomium thermophilum pre-60S ribosomal subunit - Ytm1-2electron microscopyCC—5 (best 0.89)
8I9ZCryo-EM structure of a Chaetomium thermophilum pre-60S ribosomal subunit - State Spb4electron microscopyCC—3 (best 0.89)
8PV2Chaetomium thermophilum pre-60S State 10 - pre-5S rotation with Ytm1-Erb1electron microscopyCC—2 (best 0.87)
G0SCK6AlphaFold monomer V2.0 prediction for ribosome biogenesis protein ERB1 (G0SCK6)predictedA——

Ligands

  • MG · Magnesium ion · in 1 record

Experiment against prediction

Elsewhere

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