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Heterotetramer structure of kluyveromyces lactis CSE4,H4

Analyse Heterotetramer structure of kluyveromyces lactis CSE4,H4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YFW
Type: protein
Length: 604 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone H3-like centromeric protein CSE4; Histone H4
UniProt: Q6CTI2, Q6CMU6
Pockets: 7 · best druggability 0.79

Structure

x-ray diffraction · 8 distinct chains · 68% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone H3-like centromeric protein CSE4	protein	78	69% helix, 5% strand	Q6CTI2
B	Histone H4	protein	66	71% helix, 6% strand	Q6CMU6
C	Histone H3-like centromeric protein CSE4	protein	71	72% helix, 6% strand	Q6CTI2
D	Histone H4	protein	71	66% helix, 6% strand	Q6CMU6
E	Histone H3-like centromeric protein CSE4	protein	88	67% helix, 5% strand	Q6CTI2
F	Histone H4	protein	72	69% helix, 6% strand	Q6CMU6
G	Histone H3-like centromeric protein CSE4	protein	78	69% helix, 5% strand	Q6CTI2
H	Histone H4	protein	80	60% helix, 5% strand	Q6CMU6

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	708	0.79	0.83	84	empty
2	109	0.55	0.84	24	empty
3	113	0.52	0.82	20	empty
4	129	0.52	0.80	18	empty
5	118	0.51	0.82	17	empty

Interfaces

19 interfaces between chains.

E–F · 2429 Å² buried · 17 hydrogen bonds · protein-protein
G–H · 2346 Å² buried · 23 hydrogen bonds · protein-protein
A–B · 2068 Å² buried · 13 hydrogen bonds · protein-protein
C–D · 1905 Å² buried · 14 hydrogen bonds · protein-protein
A–C · 660 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

2YFW · Heterotetramer structure of Kluyveromyces lactis Cse4,H4 · the same entry in another collection · chain H against H, TM-score 1.00
Q6CTI2 · AlphaFold monomer V2.0 prediction for histone H3-like centromeric protein CSE4 (Q6CTI2) · a predicted model of the same protein · chain E 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 Q6CTI2
Every structure of UniProt Q6CMU6
Elsewhere: RCSB PDB 2YFW · PDBe 2YFW · UniProt Q6CTI2 · UniProt Q6CMU6

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