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Structure of antigen-Fab complex with histone chaperone ASF1

Analyse Structure of antigen-Fab complex with histone chaperone ASF1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UEA
Type: protein
Length: 1,137 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fab heavy chain; Histone chaperone ASF1; Fab light chain
UniProt: P32447
Pockets: 7 · best druggability 0.75

Structure

x-ray diffraction · 5 distinct chains · 8% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fab heavy chain	protein	212	8% helix, 52% strand	—
X	Histone chaperone ASF1	protein	153	9% helix, 50% strand	P32447
H	Fab heavy chain	protein	215	9% helix, 51% strand	—
D	Histone chaperone ASF1	protein	135	6% helix, 56% strand	P32447
L, B	Fab light chain	protein	211	6% helix, 52% strand	—

Pockets

7 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	825	0.75	0.80	79	empty
2	683	0.69	0.77	56	empty
3	392	0.58	0.75	50	empty
4	329	0.54	0.74	45	empty
5	86	0.34	0.74	24	empty

Interfaces

11 interfaces between chains.

A–B · 1742 Å² buried · 15 hydrogen bonds · protein-protein
H–L · 1723 Å² buried · 16 hydrogen bonds · protein-protein
H–D · 636 Å² buried · 7 hydrogen bonds · protein-protein
A–X · 632 Å² buried · 7 hydrogen bonds · protein-protein
D–L · 354 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

5UEA · Structure of antigen-Fab complex with Histone chaperone ASF1 · the same entry in another collection · chain B against B, TM-score 1.00
P32447 · AlphaFold monomer V2.0 prediction for histone chaperone ASF1 (P32447) · a predicted model of the same protein · chain D against A, TM-score 0.97

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 P32447
Elsewhere: RCSB PDB 5UEA · PDBe 5UEA · UniProt P32447

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