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Structure of cyclin MCS2

Analyse Structure of cyclin MCS2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JKW
Type: protein
Length: 277 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclin H
UniProt: P51946
Pockets: 5 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 68% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyclin H	protein	277	68% helix, 0% strand	P51946

Pockets

5 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	178	0.61	0.83	25	empty
2	101	0.51	0.82	18	empty
3	117	0.43	0.77	18	empty
4	74	0.41	0.79	15	empty
5	56	0.41	0.81	15	empty

Compared structures

1JKW · Structure of cyclin MCS2 · the same entry in another collection · chain A against A, TM-score 1.00
P51946 · AlphaFold monomer V2.0 prediction for cyclin-H (P51946) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P51946
Elsewhere: RCSB PDB 1JKW · PDBe 1JKW · UniProt P51946

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