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Crystal structure of the run domain of human nesca

Analyse Crystal structure of the run domain of human nesca in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4GIW
Type: protein
Length: 349 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Run and SH3 domain-containing protein 1
UniProt: Q9BVN2
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 66% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Run and SH3 domain-containing protein 1	protein	179	64% helix, 8% strand	Q9BVN2
B	Run and SH3 domain-containing protein 1	protein	170	68% helix, 2% strand	Q9BVN2

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	163	0.61	0.83	24	empty
2	382	0.61	0.77	32	empty
3	58	0.47	0.84	17	empty

Interfaces

1 interface between chains.

A–B · 1021 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

4GIW · Crystal structure of the RUN domain of human NESCA · the same entry in another collection · chain A against A, TM-score 1.00
Q9BVN2 · AlphaFold monomer V2.0 prediction for run and SH3 domain-containing protein 1 (Q9BVN2) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 Q9BVN2
Elsewhere: RCSB PDB 4GIW · PDBe 4GIW · UniProt Q9BVN2

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