Research workbench

Structure of a yeast TFIIA/TBP/TATA-box DNA complex

Analyse Structure of a yeast TFIIA/TBP/TATA-box DNA complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RM1
Type: protein + DNA
Length: 433 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P13393, P32774, P32773

Structure

x-ray diffraction · 5 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D	—	dna	18	—	—
E	—	dna	18	—	—
A	—	protein	180	—	P13393
B	—	protein	101	—	P32774
C	—	protein	116	—	P32773

Compared structures

1RM1 · Structure of a Yeast TFIIA/TBP/TATA-box DNA Complex · the same entry in another collection · chain C against C, TM-score 1.00
P13393 · AlphaFold monomer V2.0 prediction for tata-box-binding protein (P13393) · a predicted model of the same protein · chain A against A, TM-score 0.99
P32774 · AlphaFold monomer V2.0 prediction for transcription initiation factor iia subunit 2… · a predicted model of the same protein · chain B against A, TM-score 0.97
P32773 · AlphaFold monomer V2.0 prediction for transcription initiation factor iia large subunit… · a predicted model of the same protein · chain C against A, TM-score 0.93

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 P13393
Every structure of UniProt P32774
Every structure of UniProt P32773
Elsewhere: RCSB PDB 1RM1 · PDBe 1RM1 · UniProt P13393 · UniProt P32774 · UniProt P32773

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