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Crystal structure of the hat-C domain of murine cstf-77

Analyse Crystal structure of the hat-C domain of murine cstf-77 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OND
Type: protein
Length: 616 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cleavage stimulation factor 77 kda subunit
UniProt: Q99LI7
Pockets: 6 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 72% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cleavage stimulation factor 77 kda subunit	protein	308	72% helix, 1% strand	Q99LI7

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1126	0.78	0.80	91	empty
2	319	0.62	0.79	40	empty
3	255	0.62	0.80	31	empty
4	65	0.32	0.75	19	empty
5	65	0.31	0.75	17	empty

Interfaces

1 interface between chains.

A–B · 2858 Å² buried · 36 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

2OND · Crystal Structure of the HAT-C domain of murine CstF-77 · the same entry in another collection · chain A against A, TM-score 1.00
Q99LI7 · AlphaFold monomer V2.0 prediction for cleavage stimulation factor subunit 3 (Q99LI7) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q99LI7
Elsewhere: RCSB PDB 2OND · PDBe 2OND · UniProt Q99LI7

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