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Crystal structure of hcf-1 self-association sequence 1

Analyse Crystal structure of hcf-1 self-association sequence 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4GO6
Type: protein
Length: 422 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hcf N-terminal chain 1; Hcf C-terminal chain 1
UniProt: P51610
Ligands: SO4
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 4 distinct chains · 2% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hcf N-terminal chain 1	protein	41	0% helix, 54% strand	P51610
B	Hcf C-terminal chain 1	protein	168	2% helix, 56% strand	P51610
C	Hcf N-terminal chain 1	protein	40	0% helix, 43% strand	P51610
D	Hcf C-terminal chain 1	protein	173	2% helix, 51% strand	P51610

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, B, D, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 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	1023	0.76	0.79	93	empty
2	124	0.54	0.82	26	empty
3	82	0.34	0.75	19	empty

Interfaces

5 interfaces between chains.

A–B · 2485 Å² buried · 36 hydrogen bonds · protein-protein
C–D · 2108 Å² buried · 39 hydrogen bonds · protein-protein
B–D · 1254 Å² buried · 17 hydrogen bonds · protein-protein
B–C · 256 Å² buried · 3 hydrogen bonds · protein-protein
A–D · 76 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

4GO6 · Crystal structure of HCF-1 self-association sequence 1 · the same entry in another collection · chain A against A, TM-score 1.00
P51610 · AlphaFold monomer V2.0 prediction for host cell factor 1 (P51610) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P51610
Elsewhere: RCSB PDB 4GO6 · PDBe 4GO6 · UniProt P51610

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