Research workbench

Redox-sensing transcriptional repressor rex

Analyse Redox-sensing transcriptional repressor rex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZZ5
Type: protein
Length: 745 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Redox-sensing transcriptional repressor rex
UniProt: Q9WY16
Pockets: 10 · best druggability 0.76

Structure

x-ray diffraction · 4 distinct chains · 48% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Redox-sensing transcriptional repressor rex	protein	200	51% helix, 20% strand	Q9WY16
B	Redox-sensing transcriptional repressor rex	protein	206	49% helix, 19% strand	Q9WY16
C	Redox-sensing transcriptional repressor rex	protein	156	44% helix, 21% strand	Q9WY16
D	Redox-sensing transcriptional repressor rex	protein	183	48% helix, 19% strand	Q9WY16

Ligands and binding sites

GOL · Glycerol · additive · 4 copies · chains A, B, C, D

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

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	98	0.76	0.96	16	GOL
2	651	0.65	0.75	74	empty
3	510	0.62	0.75	67	GOL
4	377	0.55	0.74	51	empty
5	141	0.48	0.78	23	empty

Interfaces

4 interfaces between chains.

A–B · 2603 Å² buried · 9 hydrogen bonds · protein-protein
C–D · 2310 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 227 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 203 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5ZZ5 · Redox-sensing transcriptional repressor Rex · the same entry in another collection · chain B against B, TM-score 1.00
Q9WY16 · AlphaFold monomer V2.0 prediction for redox-sensing transcriptional repressor rex 1… · a predicted model of the same protein · chain D against A, TM-score 0.96

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 Q9WY16
Elsewhere: RCSB PDB 5ZZ5 · PDBe 5ZZ5 · UniProt Q9WY16

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