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Crystal structure of ForH

Analyse Crystal structure of ForH in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6NKO
Type: protein
Length: 768 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.403
Source: Streptomyces kaniharaensis
Molecule: ForH
Pockets: 11 · best druggability 0.75

Structure

x-ray diffraction · resolution 2.403 · 4 distinct chains · 52% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ForH	protein	196	51% helix, 9% strand	—
B	ForH	protein	192	53% helix, 10% strand	—
C	ForH	protein	190	51% helix, 9% strand	—
D	ForH	protein	190	53% helix, 11% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	86	0.75	0.97	28	empty
2	545	0.68	0.78	58	empty
3	190	0.64	0.84	30	empty
4	300	0.62	0.80	30	empty
5	306	0.60	0.78	34	empty

Interfaces

5 interfaces between chains.

A–D · 2104 Å² buried · 32 hydrogen bonds · protein-protein
B–C · 2061 Å² buried · 25 hydrogen bonds · protein-protein
A–B · 822 Å² buried · 10 hydrogen bonds · protein-protein
A–C · 431 Å² buried · 8 hydrogen bonds · protein-protein
B–D · 401 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6NKO · Crystal structure of forh · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 6NKO · PDBe 6NKO

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