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Crystal structure of an inhibited fragment of ets-1

Analyse Crystal structure of an inhibited fragment of ets-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MD0
Type: protein
Length: 276 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-ets-1 protein
UniProt: P27577
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	C-ets-1 protein	protein	138	48% helix, 9% strand	P27577

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	798	0.66	0.74	56	empty
2	59	0.28	0.73	14	empty

Interfaces

1 interface between chains.

A–B · 789 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1MD0 · CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1 · the same entry in another collection · chain A against A, TM-score 1.00
P27577 · AlphaFold monomer V2.0 prediction for protein C-ets-1 (P27577) · a predicted model of the same protein · chain A against A, TM-score 0.87

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 P27577
Elsewhere: RCSB PDB 1MD0 · PDBe 1MD0 · UniProt P27577

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