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Crystal structure of the RIF1 N-terminal domain (RIF1-ntd) from saccharomyces cerevisiae

Analyse Crystal structure of the RIF1 N-terminal domain (RIF1-ntd) from saccharomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NVR
Type: protein
Length: 1,072 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Telomere length regulator protein RIF1
UniProt: P29539
Pockets: 8 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 69% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Telomere length regulator protein RIF1	protein	1072	69% helix, 0% strand	P29539

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	205	0.73	0.88	25	empty
2	315	0.67	0.81	35	empty
3	52	0.66	0.95	14	empty
4	147	0.65	0.86	27	empty
5	132	0.43	0.76	23	empty

Modifications

Observed in the structure: 22 modified (engineered).

Compared structures

5NVR · Crystal structure of the Rif1 N-terminal domain (RIF1-NTD) from Saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
P29539 · AlphaFold monomer V2.0 prediction for telomere length regulator protein RIF1 (P29539) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P29539
Elsewhere: RCSB PDB 5NVR · PDBe 5NVR · UniProt P29539

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