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Crystal structure of ASF1-Fab 12E complex

Analyse Crystal structure of ASF1-Fab 12E complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AZ2
Type: protein
Length: 1,131 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 0.72

Structure

x-ray diffraction · 6 distinct chains · 6% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fab heavy chain	protein	213	7% helix, 54% strand	—
C	Fab heavy chain	protein	214	6% helix, 53% strand	—
B	Histone chaperone ASF1	protein	136	6% helix, 57% strand	P32447
D	Histone chaperone ASF1	protein	147	8% helix, 52% strand	P32447
E	Fab light chain	protein	210	6% helix, 52% strand	—
F	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	571	0.72	0.80	60	empty
2	506	0.63	0.75	52	empty
3	478	0.60	0.75	55	empty
4	372	0.56	0.75	48	empty
5	132	0.38	0.74	21	empty

Interfaces

12 interfaces between chains.

C–E · 1746 Å² buried · 14 hydrogen bonds · protein-protein
A–F · 1741 Å² buried · 13 hydrogen bonds · protein-protein
C–D · 620 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 610 Å² buried · 5 hydrogen bonds · protein-protein
D–E · 351 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

6AZ2 · Crystal structure of Asf1-Fab 12E complex · the same entry in another collection · chain E against E, TM-score 1.00
P32447 · AlphaFold monomer V2.0 prediction for histone chaperone ASF1 (P32447) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 6AZ2 · PDBe 6AZ2 · UniProt P32447

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