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Sant domain structure of xenopus remodeling factor iswi

Analyse Sant domain structure of xenopus remodeling factor iswi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NOG
Type: protein
Length: 313 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Iswi protein
UniProt: Q6DFM0
Ligands: MG
Pockets: 6 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 61% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Iswi protein	protein	157	62% helix, 0% strand	Q6DFM0
B	Iswi protein	protein	156	61% helix, 0% strand	Q6DFM0

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	137	0.49	0.78	19	empty
2	154	0.42	0.74	22	empty
3	126	0.41	0.75	20	empty
4	58	0.40	0.81	20	empty
5	141	0.38	0.73	21	empty

Interfaces

1 interface between chains.

A–B · 715 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

2NOG · SANT Domain Structure of Xenopus Remodeling Factor ISWI · 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 Q6DFM0
Elsewhere: RCSB PDB 2NOG · PDBe 2NOG · UniProt Q6DFM0

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