Research workbench

SPT6 TSH2-RPB1 1468-1500 PT1471, PS1493

Analyse SPT6 TSH2-RPB1 1468-1500 PT1471, PS1493 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VKO
Type: protein
Length: 232 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcription elongation factor SPT6; DNA-directed RNA polymerase II subunit RPB1
EC: 2.7.7.6
UniProt: P23615, P04050

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcription elongation factor SPT6	protein	201	30% helix, 29% strand	P23615
B	DNA-directed RNA polymerase II subunit RPB1 (EC 2.7.7.6)	protein	31	10% helix, 0% strand	P04050

Ligands and binding sites

IPA · Isopropyl alcohol · additive

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

A–B · 1757 Å² buried · 30 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

5VKO · SPT6 tSH2-RPB1 1468-1500 pT1471, 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 5VKO · PDBe 5VKO · UniProt P23615 · UniProt P04050

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