Research workbench

SPT6 tSH2-RPB1 1476-1500 pS1493

Analyse SPT6 tSH2-RPB1 1476-1500 pS1493 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VKL
Type: protein
Length: 222 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.198
Source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c); SYNTHETIC CONSTRUCT
Molecule: Transcription elongation factor SPT6; DNA-directed RNA polymerase II subunit RPB1
EC: 2.7.7.6
UniProt: P23615, P04050

Structure

x-ray diffraction · resolution 2.198 · 2 distinct chains · 27% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcription elongation factor SPT6	protein	202	30% helix, 30% strand	P23615
B	DNA-directed RNA polymerase II subunit RPB1 (EC 2.7.7.6)	protein	20	0% helix, 0% strand	P04050

Interfaces

1 interface between chains.

A–B · 1229 Å² buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

5VKL · SPT6 TSH2-RPB1 1476-1500 PS1493 · the same entry in another collection · chain A against A, TM-score 1.00
P23615 · AlphaFold monomer V2.0 prediction for transcription elongation factor SPT6 (P23615) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P23615
Every structure of UniProt P04050
Elsewhere: RCSB PDB 5VKL · PDBe 5VKL · UniProt P23615 · UniProt P04050

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