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Crystal structure of a. aeolicus NLH2 gaf domain in an inactive state

Analyse Crystal structure of a. aeolicus NLH2 gaf domain in an inactive state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4G3V
Type: protein
Length: 324 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcriptional regulator NLH2
UniProt: O67661
Ligands: CL
Pockets: 1 · best druggability 0.27

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transcriptional regulator NLH2	protein	162	46% helix, 27% strand	O67661

Ligands and binding sites

CL · Chloride ion · ion · 4 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	56	0.27	0.73	13	empty

Interfaces

1 interface between chains.

A–B · 1218 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

4G3V · Crystal structure of A. Aeolicus nlh2 gaf domain in an inactive state · the same entry in another collection · chain A against A, TM-score 1.00

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 O67661
Elsewhere: RCSB PDB 4G3V · PDBe 4G3V · UniProt O67661

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