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High resolution crystal structure of the monomeric subunit-free CAF1M chaperone

Analyse High resolution crystal structure of the monomeric subunit-free CAF1M chaperone in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AY0
Type: protein
Length: 377 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein CAF1M
UniProt: P26926
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chaperone protein CAF1M	protein	188	3% helix, 51% strand	P26926
B	Chaperone protein CAF1M	protein	189	4% helix, 50% strand	P26926

Pockets

2 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	568	0.66	0.77	62	empty
2	387	0.60	0.76	64	empty

Interfaces

1 interface between chains.

A–B · 1266 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

4AY0 · High resolution crystal structure of the monomeric subunit-free Caf1M chaperone · the same entry in another collection · chain A against A, TM-score 1.00
P26926 · AlphaFold monomer V2.0 prediction for chaperone protein CAF1M (P26926) · 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 P26926
Elsewhere: RCSB PDB 4AY0 · PDBe 4AY0 · UniProt P26926

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