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Crystal structure of ffrp

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

PDB: 2ZNZ
Type: protein
Length: 1,166 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized hth-type transcriptional regulator PH1519
UniProt: O59188
Ligands: LYS
Pockets: 13 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D, E, F, G, H	Uncharacterized hth-type transcriptional regulator PH1519	protein	146	40% helix, 32% strand	O59188
C	Uncharacterized hth-type transcriptional regulator PH1519	protein	144	38% helix, 32% strand	O59188

Ligands and binding sites

LYS · Lysine · ligand · 8 copies · chains A, B, C, D, E, F, G, H

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

Pockets

13 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	222	0.73	0.89	30	empty
2	224	0.73	0.88	30	empty
3	221	0.72	0.88	30	empty
4	241	0.72	0.87	31	empty
5	80	0.40	0.78	18	empty

Interfaces

6 interfaces between chains.

G–H · 3075 Å² buried · 54 hydrogen bonds · protein-protein
A–B · 3060 Å² buried · 57 hydrogen bonds · protein-protein
E–F · 3053 Å² buried · 54 hydrogen bonds · protein-protein
C–D · 3043 Å² buried · 57 hydrogen bonds · protein-protein
A–E · 60 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

2ZNZ · Crystal structure of FFRP · the same entry in another collection · chain F against F, TM-score 1.00
O59188 · AlphaFold monomer V2.0 prediction for hth-type transcriptional regulator FL11 (O59188) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 O59188
Elsewhere: RCSB PDB 2ZNZ · PDBe 2ZNZ · UniProt O59188

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