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The crystal structure of cellular repressor of E1A- stimulated genes (creg)

Analyse The crystal structure of cellular repressor of E1A- stimulated genes (creg) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XHN
Type: protein
Length: 686 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellular repressor of E1A-stimulated genes
UniProt: O75629
Pockets: 9 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	Cellular repressor of E1A-stimulated genes	protein	172	34% helix, 30% strand	O75629
B, C	Cellular repressor of E1A-stimulated genes	protein	171	32% helix, 30% strand	O75629

Pockets

9 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	763	0.76	0.80	86	empty
2	186	0.67	0.86	25	empty
3	215	0.66	0.84	25	empty
4	196	0.65	0.84	24	empty
5	194	0.51	0.77	27	empty

Interfaces

5 interfaces between chains.

A–B · 1927 Å² buried · 20 hydrogen bonds · protein-protein
C–D · 1902 Å² buried · 19 hydrogen bonds · protein-protein
A–C · 373 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 86 Å² buried · 0 hydrogen bonds · protein-protein
A–D · 23 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified, 4 disulfide (engineered, disulfide).

Compared structures

1XHN · The crystal structure of Cellular Repressor of E1A-stimulated Genes (CREG) · the same entry in another collection · chain C against C, TM-score 1.00
O75629 · AlphaFold monomer V2.0 prediction for protein CREG1 (O75629) · a predicted model of the same protein · chain C against A, TM-score 0.99

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 O75629
Elsewhere: RCSB PDB 1XHN · PDBe 1XHN · UniProt O75629

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