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AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerases IV and V subunit 4 (Q6DBA5)

Analyse AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerases IV and V… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q6DBA5
Type: protein
Length: 205 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x2A40776e144333aa14A6Da9D7a7a28806d8c1007
Molecule: DNA-directed RNA polymerases IV and V subunit 4
UniProt: Q6DBA5

Structure

1 distinct chain · 43% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA-directed RNA polymerases IV and V subunit 4	protein	205	43% helix, 1% strand	Q6DBA5

Compared structures

8HYJ · A cryo-EM structure of KTF1-bound polymerase V transcription elongation complex · an experimental structure of the same protein · chain A against D, TM-score 0.50
8XMC · Post-translocated Pol IV transcription elongation complex · an experimental structure of the same protein · chain A against D, TM-score 0.46
8XMB · NTP-bound Pol IV transcription elongation complex · an experimental structure of the same protein · chain A against D, TM-score 0.46
8XME · Backtracked Pol IV transcription elongation complex · an experimental structure of the same protein · chain A against D, TM-score 0.46
8XMD · Pre-translocated Pol IV transcription elongation complex · an experimental structure of the same protein · chain A against D, TM-score 0.46

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q6DBA5
Elsewhere: UniProt Q6DBA5 · AlphaFold DB Q6DBA5

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