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Crystal structure of the ffrp

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

PDB: 2ZNY
Type: protein
Length: 1,168 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: ARG
Pockets: 19 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	Uncharacterized hth-type transcriptional regulator PH1519	protein	146	40% helix, 30% strand	O59188

Ligands and binding sites

ARG · Arginine · ligand · 6 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

19 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	344	0.73	0.85	42	empty
2	1086	0.73	0.77	112	empty
3	186	0.73	0.90	31	empty
4	333	0.71	0.84	44	empty
5	277	0.70	0.85	43	empty

Interfaces

17 interfaces between chains.

G–H · 3183 Å² buried · 50 hydrogen bonds · protein-protein
A–B · 3181 Å² buried · 52 hydrogen bonds · protein-protein
E–F · 3111 Å² buried · 50 hydrogen bonds · protein-protein
C–D · 3104 Å² buried · 53 hydrogen bonds · protein-protein
B–C · 570 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

2ZNY · Crystal structure of the FFRP · the same entry in another collection · chain H against H, 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 D 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 O59188
Elsewhere: RCSB PDB 2ZNY · PDBe 2ZNY · UniProt O59188

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