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Crystal structure of the RAP30/74 interaction domains of human tfiif

Analyse Crystal structure of the RAP30/74 interaction domains of human tfiif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1F3U
Type: protein
Length: 1,055 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcription initiation factor iif, beta subunit; Transcription initiation factor iif…
UniProt: P13984, P35269
Pockets: 14 · best druggability 0.70

Structure

x-ray diffraction · 5 distinct chains · 14% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, G	Transcription initiation factor iif, beta subunit	protein	118	13% helix, 48% strand	P13984
B	Transcription initiation factor iif, alpha subunit	protein	139	12% helix, 45% strand	P35269
D	Transcription initiation factor iif, alpha subunit	protein	153	17% helix, 42% strand	P35269
F	Transcription initiation factor iif, alpha subunit	protein	154	15% helix, 44% strand	P35269
H	Transcription initiation factor iif, alpha subunit	protein	137	11% helix, 44% strand	P35269

Pockets

14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	629	0.70	0.78	66	empty
2	532	0.70	0.80	54	empty
3	950	0.70	0.75	76	empty
4	823	0.69	0.76	69	empty
5	193	0.52	0.78	25	empty

Interfaces

18 interfaces between chains.

A–B · 2375 Å² buried · 40 hydrogen bonds · protein-protein
E–F · 2375 Å² buried · 44 hydrogen bonds · protein-protein
C–D · 2343 Å² buried · 39 hydrogen bonds · protein-protein
G–H · 2331 Å² buried · 39 hydrogen bonds · protein-protein
E–G · 334 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

1F3U · Crystal structure of the RAP30/74 interaction domains of human tfiif · the same entry in another collection · chain H against H, TM-score 1.00
P13984 · AlphaFold monomer V2.0 prediction for general transcription factor iif subunit 2 (P13984) · a predicted model of the same protein · chain A against A, TM-score 0.85
P35269 · AlphaFold monomer V2.0 prediction for general transcription factor iif subunit 1 (P35269) · a predicted model of the same protein · chain H against A, TM-score 0.84

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 P13984
Every structure of UniProt P35269
Elsewhere: RCSB PDB 1F3U · PDBe 1F3U · UniProt P13984 · UniProt P35269

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